Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
Identifieur interne : 002012 ( Main/Exploration ); précédent : 002011; suivant : 002013Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
Auteurs : W. R. Tulip [Australie] ; J. N. Varghese [Australie] ; A. T. Baker [Australie, États-Unis] ; A. Van Donkelaar [Australie] ; W. G. Laver [Australie] ; R. G. Webster [États-Unis] ; P. M. Colman [Australie]Source :
- 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Subtype neuraminidases, Subtypes, Subunit, Surface area, Surface regions, Tetramer interface, Thick lines, Unpublished results, Varghese, Varghese colman, Water molecule, Water molecules, Xplor, Xplor cycle.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
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000F26
- to stream Istex, to step Curation: 000F26
- to stream Istex, to step Checkpoint: 000D54
- to stream Main, to step Merge: 002111
- to stream Main, to step Curation: 002012
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title><author><name sortKey="Tulip, W R" sort="Tulip, W R" uniqKey="Tulip W" first="W. R." last="Tulip">W. R. Tulip</name></author><author><name sortKey="Varghese, J N" sort="Varghese, J N" uniqKey="Varghese J" first="J. N." last="Varghese">J. N. Varghese</name></author><author><name sortKey="Baker, A T" sort="Baker, A T" uniqKey="Baker A" first="A. T." last="Baker">A. T. Baker</name></author><author><name sortKey="Van Donkelaar, A" sort="Van Donkelaar, A" uniqKey="Van Donkelaar A" first="A." last="Van Donkelaar">A. Van Donkelaar</name></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></author><author><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D7BA73AEBDA5E7E2E85CF78CC51372E05A90176D</idno><date when="1991" year="1991">1991</date><idno type="doi">10.1016/0022-2836(91)80069-7</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-L7B0ZNM2-W/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000F26</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000F26</idno><idno type="wicri:Area/Istex/Curation">000F26</idno><idno type="wicri:Area/Istex/Checkpoint">000D54</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000D54</idno><idno type="wicri:doubleKey">0022-2836:1991:Tulip W:refined:atomic:structures</idno><idno type="wicri:Area/Main/Merge">002111</idno><idno type="wicri:Area/Main/Curation">002012</idno><idno type="wicri:Area/Main/Exploration">002012</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title><author><name sortKey="Tulip, W R" sort="Tulip, W R" uniqKey="Tulip W" first="W. R." last="Tulip">W. R. Tulip</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052</wicri:regionArea><wicri:noRegion>Parkville 3052</wicri:noRegion></affiliation></author><author><name sortKey="Varghese, J N" sort="Varghese, J N" uniqKey="Varghese J" first="J. N." last="Varghese">J. N. Varghese</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052</wicri:regionArea><wicri:noRegion>Parkville 3052</wicri:noRegion></affiliation></author><author><name sortKey="Baker, A T" sort="Baker, A T" uniqKey="Baker A" first="A. T." last="Baker">A. T. Baker</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052</wicri:regionArea><wicri:noRegion>Parkville 3052</wicri:noRegion></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>† Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403</wicri:regionArea><placeName><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Van Donkelaar, A" sort="Van Donkelaar, A" uniqKey="Van Donkelaar A" first="A." last="Van Donkelaar">A. Van Donkelaar</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052</wicri:regionArea><wicri:noRegion>Parkville 3052</wicri:noRegion></affiliation></author><author><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>John Curtin School of Medical Research Australian National University, Canberra 2601</wicri:regionArea><wicri:noRegion>Canberra 2601</wicri:noRegion></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 wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>St Jude Children's Research Hospital Memphis, TN 38101</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></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 wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Division of Biomolecular Engineering 343 Royal Parade, Parkville 3052</wicri:regionArea><wicri:noRegion>Parkville 3052</wicri:noRegion></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><affiliations><list><country><li>Australie</li><li>États-Unis</li></country><region><li>Oregon</li><li>Tennessee</li></region></list><tree><country name="Australie"><noRegion><name sortKey="Tulip, W R" sort="Tulip, W R" uniqKey="Tulip W" first="W. R." last="Tulip">W. R. Tulip</name></noRegion><name sortKey="Baker, A T" sort="Baker, A T" uniqKey="Baker A" first="A. T." last="Baker">A. T. Baker</name><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name><name sortKey="Van Donkelaar, A" sort="Van Donkelaar, A" uniqKey="Van Donkelaar A" first="A." last="Van Donkelaar">A. Van Donkelaar</name><name sortKey="Varghese, J N" sort="Varghese, J N" uniqKey="Varghese J" first="J. N." last="Varghese">J. N. Varghese</name></country><country name="États-Unis"><region name="Oregon"><name sortKey="Baker, A T" sort="Baker, A T" uniqKey="Baker A" first="A. T." last="Baker">A. T. Baker</name></region><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002012 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002012 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:D7BA73AEBDA5E7E2E85CF78CC51372E05A90176D
|texte= Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
}}
| This area was generated with Dilib version V0.6.33. |  |