Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
Identifieur interne : 000F26 ( Istex/Corpus ); précédent : 000F25; suivant : 000F27Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
Auteurs : W. R. Tulip ; J. N. Varghese ; A. T. Baker ; A. Van Donkelaar ; W. G. Laver ; R. G. Webster ; P. M. ColmanSource :
- Journal of Molecular Biology [ 0022-2836 ] ; 1991.
English descriptors
- Teeft :
- Active site, Amino, Antibody binding sites, Antigenic, Antigenic variation, Average temperature factors, Avian influenza virus, Bond angles, Bond lengths, Bottom right, Carbohydrate, Colman, Complex structure, Contour levels, Data collection, Difference maps, Different position, Direct evidence, Disease virus, Electron density, Energy refinement, Film packs, Immune recognition, Influenza, Influenza virus, Influenza virus neuraminidase, Injluenza virus, Isotropic temperature factor refinement, Large probe, Largest difference, Largest uninterpretable peaks, Lattice contacts, Laver, Molecular dynamics refinement, Monoclonal antibodies, Mutant, Mutation, Neuraminidase, Neuraminidase structure, Novel mechanism, Present address, Protein atoms, Putative calcium, Radius probe, Ramachandran plot, Reference structure, Refinement, Residue, Residue number, Second antibody, Second cycle, Sheet strands, Structural studies, Structure factors, Substitution, Subtype, Subtype neuraminidase, Subtype neuraminidases, Subtypes, Subunit, Surface area, Surface regions, Tetramer interface, Thick lines, Unpublished results, Varghese, Varghese colman, Water molecule, Water molecules, Xplor, Xplor cycle.
Abstract
Abstract: The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2 or more.
Url:
DOI: 10.1016/0022-2836(91)80069-7
Links to Exploration step
ISTEX:D7BA73AEBDA5E7E2E85CF78CC51372E05A90176DLe document en format XML
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Laver</name><affiliation><mods:affiliation>John Curtin School of Medical Research Australian National University, Canberra 2601, Australia</mods:affiliation></affiliation></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name><affiliation><mods:affiliation>St Jude Children's Research Hospital Memphis, TN 38101, U.S.A.</mods:affiliation></affiliation></author><author><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name><affiliation><mods:affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="ISSN">0022-2836</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">221</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="487">487</biblScope><biblScope unit="page" to="497">497</biblScope></imprint><idno type="ISSN">0022-2836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2836</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Active site</term><term>Amino</term><term>Antibody binding sites</term><term>Antigenic</term><term>Antigenic variation</term><term>Average temperature factors</term><term>Avian influenza virus</term><term>Bond angles</term><term>Bond lengths</term><term>Bottom right</term><term>Carbohydrate</term><term>Colman</term><term>Complex structure</term><term>Contour levels</term><term>Data collection</term><term>Difference maps</term><term>Different position</term><term>Direct evidence</term><term>Disease virus</term><term>Electron density</term><term>Energy refinement</term><term>Film packs</term><term>Immune recognition</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Injluenza virus</term><term>Isotropic temperature factor refinement</term><term>Large probe</term><term>Largest difference</term><term>Largest uninterpretable peaks</term><term>Lattice contacts</term><term>Laver</term><term>Molecular dynamics refinement</term><term>Monoclonal antibodies</term><term>Mutant</term><term>Mutation</term><term>Neuraminidase</term><term>Neuraminidase structure</term><term>Novel mechanism</term><term>Present address</term><term>Protein atoms</term><term>Putative calcium</term><term>Radius probe</term><term>Ramachandran plot</term><term>Reference structure</term><term>Refinement</term><term>Residue</term><term>Residue number</term><term>Second antibody</term><term>Second cycle</term><term>Sheet strands</term><term>Structural studies</term><term>Structure factors</term><term>Substitution</term><term>Subtype</term><term>Subtype neuraminidase</term><term>Subtype neuraminidases</term><term>Subtypes</term><term>Subunit</term><term>Surface area</term><term>Surface regions</term><term>Tetramer interface</term><term>Thick lines</term><term>Unpublished results</term><term>Varghese</term><term>Varghese colman</term><term>Water molecule</term><term>Water molecules</term><term>Xplor</term><term>Xplor cycle</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2 or more.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>mutant</json:string><json:string>varghese</json:string><json:string>laver</json:string><json:string>xplor</json:string><json:string>antigenic</json:string><json:string>mutation</json:string><json:string>subunit</json:string><json:string>varghese colman</json:string><json:string>unpublished results</json:string><json:string>influenza</json:string><json:string>surface area</json:string><json:string>contour levels</json:string><json:string>difference maps</json:string><json:string>colman</json:string><json:string>antigenic variation</json:string><json:string>influenza virus neuraminidase</json:string><json:string>reference structure</json:string><json:string>active site</json:string><json:string>subtype neuraminidase</json:string><json:string>carbohydrate</json:string><json:string>amino</json:string><json:string>subtypes</json:string><json:string>energy refinement</json:string><json:string>injluenza virus</json:string><json:string>disease virus</json:string><json:string>influenza virus</json:string><json:string>structure factors</json:string><json:string>electron density</json:string><json:string>neuraminidase structure</json:string><json:string>largest difference</json:string><json:string>thick lines</json:string><json:string>data collection</json:string><json:string>residue</json:string><json:string>subtype</json:string><json:string>refinement</json:string><json:string>bond lengths</json:string><json:string>second cycle</json:string><json:string>subtype neuraminidases</json:string><json:string>putative calcium</json:string><json:string>ramachandran plot</json:string><json:string>bond angles</json:string><json:string>monoclonal antibodies</json:string><json:string>water molecules</json:string><json:string>tetramer interface</json:string><json:string>average temperature factors</json:string><json:string>protein atoms</json:string><json:string>immune recognition</json:string><json:string>xplor cycle</json:string><json:string>film packs</json:string><json:string>largest uninterpretable peaks</json:string><json:string>water molecule</json:string><json:string>isotropic temperature factor refinement</json:string><json:string>avian influenza virus</json:string><json:string>molecular dynamics refinement</json:string><json:string>radius probe</json:string><json:string>lattice contacts</json:string><json:string>antibody binding sites</json:string><json:string>residue number</json:string><json:string>sheet strands</json:string><json:string>present address</json:string><json:string>large probe</json:string><json:string>direct evidence</json:string><json:string>structural studies</json:string><json:string>different position</json:string><json:string>bottom right</json:string><json:string>second antibody</json:string><json:string>novel mechanism</json:string><json:string>surface regions</json:string><json:string>complex structure</json:string><json:string>substitution</json:string></teeft></keywords><author><json:item><name>W.R. Tulip</name><affiliations><json:string>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</json:string></affiliations></json:item><json:item><name>J.N. Varghese</name><affiliations><json:string>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</json:string></affiliations></json:item><json:item><name>A.T. Baker</name><affiliations><json:string>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</json:string><json:string>† Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, U.S.A.</json:string></affiliations></json:item><json:item><name>A. van Donkelaar</name><affiliations><json:string>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</json:string></affiliations></json:item><json:item><name>W.G. Laver</name><affiliations><json:string>John Curtin School of Medical Research Australian National University, Canberra 2601, Australia</json:string></affiliations></json:item><json:item><name>R.G. Webster</name><affiliations><json:string>St Jude Children's Research Hospital Memphis, TN 38101, U.S.A.</json:string></affiliations></json:item><json:item><name>P.M. Colman</name><affiliations><json:string>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>influenza</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neuraminidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>refined structure</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>antigenicity</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mutants</value></json:item></subject><arkIstex>ark:/67375/6H6-L7B0ZNM2-W</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2 or more.</abstract><qualityIndicators><score>8.644</score><pdfWordCount>5222</pdfWordCount><pdfCharCount>34407</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>598 x 842 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>137</abstractWordCount><abstractCharCount>892</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title><pmid><json:string>1920429</json:string></pmid><pii><json:string>0022-2836(91)80069-7</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Cold Spring Harbor Symp. Quant. Biol.</title><language><json:string>unknown</json:string></language><volume>54</volume><pages><first>247</first><last>255</last></pages></serie><host><title>Journal of Molecular Biology</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><issn><json:string>0022-2836</json:string></issn><pii><json:string>S0022-2836(00)X0503-7</json:string></pii><volume>221</volume><issue>2</issue><pages><first>487</first><last>497</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1991</json:string></date><geogName></geogName><orgName><json:string>CSIRO Institute of Industrial Technologies Postgraduate Studentship</json:string><json:string>Institute of Molecular Biology, University of Oregon, Eugene, OR</json:string><json:string>American Lebanese Syrian Associated Charities</json:string><json:string>National Institutes of Health</json:string><json:string>Medical Research Australian National University, Canberra</json:string><json:string>Research Hospital St Memphis, TN</json:string><json:string>Cancer Centre Support</json:string><json:string>CORE</json:string></orgName><orgName_funder><json:string>Cancer Centre Support</json:string><json:string>CORE</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>A. van Donkelaar</json:string><json:string>R.G.W. Deposition</json:string><json:string>W. R. Tulip</json:string><json:string>A. T. BakerIS</json:string><json:string>R. G. Webster</json:string><json:string>P. M. Colman</json:string><json:string>Data</json:string><json:string>W. G. Laver</json:string><json:string>A. Ir</json:string><json:string>Jude Children</json:string><json:string>Curtin School</json:string><json:string>Paul Davis</json:string></persName><placeName><json:string>Australia</json:string><json:string>Antigenicity</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Acharya et al., 1989</json:string><json:string>Brunger, 1988</json:string><json:string>Baker et al. (1987)</json:string><json:string>Knossow et al., 1984</json:string><json:string>Parry et al. (1990)</json:string><json:string>Amit et al., 1986</json:string><json:string>W. R.Tulip et al.</json:string><json:string>Air et al., 1985, 1987</json:string><json:string>Webster et al., 1987</json:string><json:string>Colman, 1989</json:string><json:string>Tulip et al.</json:string><json:string>Steigemann, 1974</json:string><json:string>W. R. Tulip et al.</json:string><json:string>Gelin & Karplus, 1979</json:string><json:string>Colman et al., 1983</json:string><json:string>Tainer et al. (1985)</json:string><json:string>Colman, 1988</json:string><json:string>Novotny et al., 1986</json:string><json:string>Hendrickson & Konnert, 1981</json:string><json:string>Varghese & Colman, 1991</json:string><json:string>Varghese et al., 1983</json:string><json:string>Colman et al., 1987</json:string><json:string>Rossmann, 1989</json:string><json:string>Varghese et al., 1988</json:string><json:string>Laver et al., 1984</json:string><json:string>Harley et al., 1989</json:string><json:string>Baker et al., 1987</json:string><json:string>Laver, 1978</json:string><json:string>Air et al., 1989</json:string><json:string>Connolly, 1983</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-L7B0ZNM2-W</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - microbiologie</json:string></inist></categories><publicationDate>1991</publicationDate><copyrightDate>1991</copyrightDate><doi><json:string>10.1016/0022-2836(91)80069-7</json:string></doi><id>D7BA73AEBDA5E7E2E85CF78CC51372E05A90176D</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1991</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>Edited by R. Huber</note><note type="content">Section title: Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title><author xml:id="author-0000"><persName><forename type="first">W.R.</forename><surname>Tulip</surname></persName><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation></author><author xml:id="author-0001"><persName><forename type="first">J.N.</forename><surname>Varghese</surname></persName><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation></author><author xml:id="author-0002"><persName><forename type="first">A.T.</forename><surname>Baker</surname></persName><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><affiliation>† Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, U.S.A.</affiliation></author><author xml:id="author-0003"><persName><forename type="first">A.</forename><surname>van Donkelaar</surname></persName><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation></author><author xml:id="author-0004"><persName><forename type="first">W.G.</forename><surname>Laver</surname></persName><affiliation>John Curtin School of Medical Research Australian National University, Canberra 2601, Australia</affiliation></author><author xml:id="author-0005"><persName><forename type="first">R.G.</forename><surname>Webster</surname></persName><affiliation>St Jude Children's Research Hospital Memphis, TN 38101, U.S.A.</affiliation></author><author xml:id="author-0006"><persName><forename type="first">P.M.</forename><surname>Colman</surname></persName><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation></author><idno type="istex">D7BA73AEBDA5E7E2E85CF78CC51372E05A90176D</idno><idno type="ark">ark:/67375/6H6-L7B0ZNM2-W</idno><idno type="DOI">10.1016/0022-2836(91)80069-7</idno><idno type="PII">0022-2836(91)80069-7</idno></analytic><monogr><title level="j">Journal of Molecular Biology</title><title level="j" type="abbrev">YJMBI</title><idno type="pISSN">0022-2836</idno><idno type="PII">S0022-2836(00)X0503-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991"></date><biblScope unit="volume">221</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="487">487</biblScope><biblScope unit="page" to="497">497</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1991</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2 or more.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>influenza</term></item><item><term>neuraminidase</term></item><item><term>refined structure</term></item><item><term>antigenicity</term></item><item><term>mutants</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1991">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YJMBI</jid><aid>91800697</aid><ce:pii>0022-2836(91)80069-7</ce:pii><ce:doi>10.1016/0022-2836(91)80069-7</ce:doi><ce:copyright type="unknown" year="1991"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</ce:title><ce:author-group><ce:author><ce:given-name>W.R.</ce:given-name><ce:surname>Tulip</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.N.</ce:given-name><ce:surname>Varghese</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.T.</ce:given-name><ce:surname>Baker</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.</ce:given-name><ce:surname>van Donkelaar</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>W.G.</ce:given-name><ce:surname>Laver</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>R.G.</ce:given-name><ce:surname>Webster</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>P.M.</ce:given-name><ce:surname>Colman</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>John Curtin School of Medical Research Australian National University, Canberra 2601, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>St Jude Children's Research Hospital Memphis, TN 38101, U.S.A.</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>†</ce:label><ce:note-para>Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, U.S.A.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="31" month="1" year="1991"></ce:date-received><ce:date-accepted day="13" month="5" year="1991"></ce:date-accepted><ce:miscellaneous>Edited by R. Huber</ce:miscellaneous><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an <ce:italic>R</ce:italic>-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å<ce:sup>2</ce:sup> or more.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>influenza</ce:text></ce:keyword><ce:keyword><ce:text>neuraminidase</ce:text></ce:keyword><ce:keyword><ce:text>refined structure</ce:text></ce:keyword><ce:keyword><ce:text>antigenicity</ce:text></ce:keyword><ce:keyword><ce:text>mutants</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title></titleInfo><name type="personal"><namePart type="given">W.R.</namePart><namePart type="family">Tulip</namePart><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.N.</namePart><namePart type="family">Varghese</namePart><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.T.</namePart><namePart type="family">Baker</namePart><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><affiliation>† Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">van Donkelaar</namePart><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.G.</namePart><namePart type="family">Laver</namePart><affiliation>John Curtin School of Medical Research Australian National University, Canberra 2601, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.G.</namePart><namePart type="family">Webster</namePart><affiliation>St Jude Children's Research Hospital Memphis, TN 38101, U.S.A.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P.M.</namePart><namePart type="family">Colman</namePart><affiliation>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0·172 for data in the resolution range 6·0 to 2·2 Å. The r.m.s. deviation from ideal values of bond lengths is 0·014 Å. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 Å2 or more.</abstract><note>Edited by R. Huber</note><note type="content">Section title: Article</note><subject><genre>Keywords</genre><topic>influenza</topic><topic>neuraminidase</topic><topic>refined structure</topic><topic>antigenicity</topic><topic>mutants</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Molecular Biology</title></titleInfo><titleInfo type="abbreviated"><title>YJMBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued></originInfo><identifier type="ISSN">0022-2836</identifier><identifier type="PII">S0022-2836(00)X0503-7</identifier><part><date>1991</date><detail type="volume"><number>221</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>361</start><end>728</end></extent><extent unit="pages"><start>487</start><end>497</end></extent></part></relatedItem><identifier type="istex">D7BA73AEBDA5E7E2E85CF78CC51372E05A90176D</identifier><identifier type="ark">ark:/67375/6H6-L7B0ZNM2-W</identifier><identifier type="DOI">10.1016/0022-2836(91)80069-7</identifier><identifier type="PII">0022-2836(91)80069-7</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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