The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
Identifieur interne : 002590 ( Istex/Corpus ); précédent : 002589; suivant : 002591The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
Auteurs : Dean R. Madden ; Joan C. Gorga ; Jack L. Strominger ; Don C. WileySource :
- Cell [ 0092-8674 ] ; 1992.
English descriptors
- Teeft :
- Acta, Acta cryst, Additional water molecules, Amino acids, Ankylosing spondylitis, Arginine, Arginine guanidinium group, Arginine side chain, Asymmetric unit, Binding cleft, Binding interactions, Binding site, Biol, Bjorkman, Carbonyl oxygen, Cell surface, Chains, Cleft, Concave surface, Conformation, Cryst, Crystal contact, Crystal structures, Disease association, Electron density, Electron density maps, Gorga, Harvest buffer, Heavy chain, Helix, Histocompatibility, Histocompatibility antigens, Hydrogen bond, Hydrogen bonds, Immunol, Jardetzky, Main chain, Major histocompatibility, Model building, Molecule, Other class, Parham, Peptide, Peptide atoms, Peptide binding, Peptide electron density, Peptide model, Peptide population, Peptide residues, Peptide side chains, Peptide termini, Program hydraster, Refinement, Residue, Room temperature, Rrikaitlk, Saper, Sequence variability, Side chain, Side chains, Sodium azide, Strominger, Structure factor amplitudes, Subtypes, Surface area, Terminus, Tight peptide binding, Townsend, Unpublished data, Water molecule, Water molecules.
Abstract
Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
Url:
DOI: 10.1016/0092-8674(92)90252-8
Links to Exploration step
ISTEX:BE003DCBA8FF6531C6F1328ED43276A9BCF1EC58Le document en format XML
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Madden</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Committee on Higher Degrees in Biophysics Harvard University Cambridge, Massachusetts 02138 USA</mods:affiliation></affiliation></author><author><name sortKey="Gorga, Joan C" sort="Gorga, Joan C" uniqKey="Gorga J" first="Joan C." last="Gorga">Joan C. Gorga</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>† Present address: 6130 Rangos Building, Children's Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, Pennsylvania 15213.</mods:affiliation></affiliation></author><author><name sortKey="Strominger, Jack L" sort="Strominger, Jack L" uniqKey="Strominger J" first="Jack L." last="Strominger">Jack L. 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Wiley</name><affiliation><mods:affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts 02138 USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">70</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1035">1035</biblScope><biblScope unit="page" to="1048">1048</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acta</term><term>Acta cryst</term><term>Additional water molecules</term><term>Amino acids</term><term>Ankylosing spondylitis</term><term>Arginine</term><term>Arginine guanidinium group</term><term>Arginine side chain</term><term>Asymmetric unit</term><term>Binding cleft</term><term>Binding interactions</term><term>Binding site</term><term>Biol</term><term>Bjorkman</term><term>Carbonyl oxygen</term><term>Cell surface</term><term>Chains</term><term>Cleft</term><term>Concave surface</term><term>Conformation</term><term>Cryst</term><term>Crystal contact</term><term>Crystal structures</term><term>Disease association</term><term>Electron density</term><term>Electron density maps</term><term>Gorga</term><term>Harvest buffer</term><term>Heavy chain</term><term>Helix</term><term>Histocompatibility</term><term>Histocompatibility antigens</term><term>Hydrogen bond</term><term>Hydrogen bonds</term><term>Immunol</term><term>Jardetzky</term><term>Main chain</term><term>Major histocompatibility</term><term>Model building</term><term>Molecule</term><term>Other class</term><term>Parham</term><term>Peptide</term><term>Peptide atoms</term><term>Peptide binding</term><term>Peptide electron density</term><term>Peptide model</term><term>Peptide population</term><term>Peptide residues</term><term>Peptide side chains</term><term>Peptide termini</term><term>Program hydraster</term><term>Refinement</term><term>Residue</term><term>Room temperature</term><term>Rrikaitlk</term><term>Saper</term><term>Sequence variability</term><term>Side chain</term><term>Side chains</term><term>Sodium azide</term><term>Strominger</term><term>Structure factor amplitudes</term><term>Subtypes</term><term>Surface area</term><term>Terminus</term><term>Tight peptide binding</term><term>Townsend</term><term>Unpublished data</term><term>Water molecule</term><term>Water molecules</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>side chains</json:string><json:string>electron density</json:string><json:string>arginine</json:string><json:string>parham</json:string><json:string>peptide model</json:string><json:string>water molecules</json:string><json:string>jardetzky</json:string><json:string>hydrogen bonds</json:string><json:string>helix</json:string><json:string>histocompatibility</json:string><json:string>cryst</json:string><json:string>strominger</json:string><json:string>rrikaitlk</json:string><json:string>saper</json:string><json:string>peptide termini</json:string><json:string>side 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image</json:string><json:string>transgenic rats</json:string><json:string>high levels</json:string><json:string>howard hughes</json:string><json:string>salt bridge</json:string><json:string>atom coloring</json:string><json:string>waals contacts</json:string><json:string>papain cleavage</json:string><json:string>cell membranes</json:string><json:string>experimental procedures</json:string><json:string>several peptide side chains</json:string><json:string>sequence araaaaaaa</json:string><json:string>crystallographic refinement</json:string><json:string>standard deviation</json:string><json:string>thin film</json:string><json:string>space group</json:string><json:string>side view</json:string><json:string>structural evidence</json:string><json:string>final stage</json:string><json:string>molecular replacement</json:string><json:string>atomic model</json:string><json:string>factor refinement</json:string><json:string>refined temperature factors</json:string><json:string>clear electron density</json:string><json:string>final stages</json:string><json:string>standard rotamers</json:string><json:string>final model</json:string><json:string>program access</json:string><json:string>contact surface</json:string><json:string>self peptides</json:string><json:string>diffraction data</json:string><json:string>anchor residues</json:string><json:string>endogenous peptides</json:string><json:string>peptides figure</json:string><json:string>peptide model rrikaitlk</json:string><json:string>several diseases</json:string><json:string>temperature factors</json:string></teeft></keywords><author><json:item><name>Dean R. Madden</name><affiliations><json:string>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</json:string><json:string>Committee on Higher Degrees in Biophysics Harvard University Cambridge, Massachusetts 02138 USA</json:string></affiliations></json:item><json:item><name>Joan C. Gorga</name><affiliations><json:string>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</json:string><json:string>† Present address: 6130 Rangos Building, Children's Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, Pennsylvania 15213.</json:string></affiliations></json:item><json:item><name>Jack L. Strominger</name><affiliations><json:string>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</json:string></affiliations></json:item><json:item><name>Don C. Wiley</name><affiliations><json:string>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</json:string><json:string>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts 02138 USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-2C95BCL6-8</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</abstract><qualityIndicators><score>9.076</score><pdfWordCount>9155</pdfWordCount><pdfCharCount>59304</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>14</pdfPageCount><pdfPageSize>576.24 x 828.12 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>173</abstractWordCount><abstractCharCount>1135</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</title><pmid><json:string>1525820</json:string></pmid><pii><json:string>0092-8674(92)90252-8</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>87</volume><pages><first>2137</first><last>2141</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1992</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0334-0</json:string></pii><volume>70</volume><issue>6</issue><pages><first>1035</first><last>1048</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1992</json:string><json:string>2003</json:string></date><geogName></geogName><orgName><json:string>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts</json:string><json:string>Medical Foundation/Charles A</json:string><json:string>Committee on Higher Degrees</json:string><json:string>Pittsburgh Supercomputer Center</json:string><json:string>National Institutes of Health</json:string><json:string>D. R. M.</json:string></orgName><orgName_funder><json:string>National Institutes of Health</json:string><json:string>D. R. M.</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Polina Klimovitsky</json:string><json:string>T. S. Jardetzky</json:string><json:string>Kristine Svenson</json:string><json:string>NED TrD</json:string><json:string>Constance Garnett</json:string><json:string>S. RowlandJones</json:string><json:string>Anastasia Haykov</json:string><json:string>Jack L. Strominger</json:string><json:string>C. Guo</json:string><json:string>The</json:string><json:string>A. Model</json:string><json:string>F. M. Richards</json:string><json:string>M. L. Silver</json:string><json:string>M. D. Handschumacher</json:string><json:string>Mia Frayser</json:string><json:string>Joan C. Gorga</json:string><json:string>A. McMichael</json:string><json:string>Don C. Wiley</json:string><json:string>Richard Crouse</json:string><json:string>W. S. Lane</json:string><json:string>A. Residues</json:string><json:string>C.Guo</json:string><json:string>S. J. Remington</json:string><json:string>T. Skarzynski</json:string></persName><placeName></placeName><ref_url></ref_url><ref_bibl><json:string>Benjamin and Parham, 1990</json:string><json:string>reviewed in DeMars and Spies, 1992</json:string><json:string>Ponder and Richards, 1987</json:string><json:string>reviewed in Davis, 1990</json:string><json:string>Henderson et al., 1992</json:string><json:string>Latron et al., 1992</json:string><json:string>Durbin et al., 1986</json:string><json:string>Chen and Parham, 1989</json:string><json:string>Hermans and McQueen, 1974</json:string><json:string>DeMars and Spies, 1992</json:string><json:string>Wei and Cresswell, 1992</json:string><json:string>Ezquerra et al., 1985</json:string><json:string>reviewed in Khan, 1987</json:string><json:string>Buxton et al. 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(1991)</json:string><json:string>Turner et al., 1975</json:string><json:string>reviewed in Benjamin and Parham, 1990</json:string><json:string>Jones and Thirup, 1986</json:string><json:string>Salter et al., 19891</json:string><json:string>Jones et al., 1991</json:string><json:string>Johnson, 1965</json:string><json:string>BreurVriesendorp et al., 1987</json:string><json:string>Hedrick et al., 1991</json:string><json:string>Choo et al., 1991</json:string><json:string>Fremont et al., 1992</json:string><json:string>Crowther and Blow, 1967</json:string><json:string>Madden and Wiley, 1992</json:string><json:string>Blum et al., 1987</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-2C95BCL6-8</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</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 - developmental 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 - General Biochemistry, Genetics and 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></inist></categories><publicationDate>1992</publicationDate><copyrightDate>1992</copyrightDate><doi><json:string>10.1016/0092-8674(92)90252-8</json:string></doi><id>BE003DCBA8FF6531C6F1328ED43276A9BCF1EC58</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2C95BCL6-8/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2C95BCL6-8/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-2C95BCL6-8/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</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>1992</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 type="content">Section title: Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</title><author xml:id="author-0000"><persName><forename type="first">Dean R.</forename><surname>Madden</surname></persName><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>Committee on Higher Degrees in Biophysics Harvard University Cambridge, Massachusetts 02138 USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Joan C.</forename><surname>Gorga</surname></persName><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>† Present address: 6130 Rangos Building, Children's Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, Pennsylvania 15213.</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Jack L.</forename><surname>Strominger</surname></persName><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Don C.</forename><surname>Wiley</surname></persName><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts 02138 USA</affiliation></author><idno type="istex">BE003DCBA8FF6531C6F1328ED43276A9BCF1EC58</idno><idno type="ark">ark:/67375/6H6-2C95BCL6-8</idno><idno type="DOI">10.1016/0092-8674(92)90252-8</idno><idno type="PII">0092-8674(92)90252-8</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0334-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992"></date><biblScope unit="volume">70</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1035">1035</biblScope><biblScope unit="page" to="1048">1048</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1992</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</p></abstract></profileDesc><revisionDesc><change when="1992-08-03">Modified</change><change when="1992">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-2C95BCL6-8/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>CELL</jid><aid>92902528</aid><ce:pii>0092-8674(92)90252-8</ce:pii><ce:doi>10.1016/0092-8674(92)90252-8</ce:doi><ce:copyright type="unknown" year="1992"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</ce:title><ce:author-group><ce:author><ce:given-name>Dean R.</ce:given-name><ce:surname>Madden</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>§</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Joan C.</ce:given-name><ce:surname>Gorga</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jack L.</ce:given-name><ce:surname>Strominger</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Don C.</ce:given-name><ce:surname>Wiley</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>★</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Committee on Higher Degrees in Biophysics Harvard University Cambridge, Massachusetts 02138 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts 02138 USA</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>†</ce:label><ce:note-para>Present address: 6130 Rangos Building, Children's Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, Pennsylvania 15213.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="20" month="7" year="1992"></ce:date-received><ce:date-revised day="3" month="8" year="1992"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC</title></titleInfo><name type="personal"><namePart type="given">Dean R.</namePart><namePart type="family">Madden</namePart><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>Committee on Higher Degrees in Biophysics Harvard University Cambridge, Massachusetts 02138 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Joan C.</namePart><namePart type="family">Gorga</namePart><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>† Present address: 6130 Rangos Building, Children's Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, Pennsylvania 15213.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jack L.</namePart><namePart type="family">Strominger</namePart><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Don C.</namePart><namePart type="family">Wiley</namePart><affiliation>Department of Biochemistry and Molecular Biology Harvard University Cambridge, Massachusetts 02138 USA</affiliation><affiliation>Howard Hughes Medical Institute Harvard University Cambridge, Massachusetts 02138 USA</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">1992</dateIssued><dateModified encoding="w3cdtf">1992-08-03</dateModified><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</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">1992</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0334-0</identifier><part><date>1992</date><detail type="volume"><number>70</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="issue-pages"><start>869</start><end>1068</end></extent><extent unit="pages"><start>1035</start><end>1048</end></extent></part></relatedItem><identifier type="istex">BE003DCBA8FF6531C6F1328ED43276A9BCF1EC58</identifier><identifier type="ark">ark:/67375/6H6-2C95BCL6-8</identifier><identifier type="DOI">10.1016/0092-8674(92)90252-8</identifier><identifier type="PII">0092-8674(92)90252-8</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:/67375/6H6-2C95BCL6-8/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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