The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions...
Gespeichert in:
| Veröffentlicht in: | Nature (London) 1987-10, Vol.329 (6139), p.512-518 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 518 |
|---|---|
| container_issue | 6139 |
| container_start_page | 512 |
| container_title | Nature (London) |
| container_volume | 329 |
| creator | BJORKMAN, P. J SAPER, M. A SAMRAOUI, B BENNETT, W. S STROMINGER, J. L WILEY, D. C |
| description | Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens. |
| doi_str_mv | 10.1038/329512a0 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_81034398</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>21180367</sourcerecordid><originalsourceid>FETCH-LOGICAL-c427t-3052ef419b286f4ac204c752841481a3ac60b0c0a090deac5a78b733003721913</originalsourceid><addsrcrecordid>eNqFkU1LAzEQhoMoWqvgHxCCiHhZnXxtkqMUPwqCl3pesml2jWyTmmwP_nsjVg9eepph3oeXmXkROiNwQ4CpW0a1INTAHpoQLuuK10ruowkAVRUoVh-h45zfAUAQyQ_RIeWcKSEmqFu8OdzF5HwfsAmj713ArQ9LH3qc_ejKcIkX2LphwMnZ2Ac_-hhK35eSceywHUzOeI7ffB6jjau1GX3rBz9-_jrmE3TQmSG7022doteH-8XsqXp-eZzP7p4ry6kcKwaCuo4T3VJVd9xYCtxKQRUnXBHDjK2hBQsGNCydscJI1UrGAJikRBM2RVc_vusUPzYuj83K5-_dTXBxkxtVvsWZVjtBVlMJWu12pIQoYLXcCRKuJaFaF_DiH_geNymUtzTlXA6a1aJA1z-QTTHn5LpmnfzKpM-GQPMdefMbeUHPt36bduWWf-A246JfbnWTrRm6ZIL1-Q-TgnDKKPsCDsKwRg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>204409365</pqid></control><display><type>article</type><title>The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens</title><source>MEDLINE</source><source>Nature</source><source>Springer Nature - Complete Springer Journals</source><creator>BJORKMAN, P. J ; SAPER, M. A ; SAMRAOUI, B ; BENNETT, W. S ; STROMINGER, J. L ; WILEY, D. C</creator><creatorcontrib>BJORKMAN, P. J ; SAPER, M. A ; SAMRAOUI, B ; BENNETT, W. S ; STROMINGER, J. L ; WILEY, D. C</creatorcontrib><description>Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/329512a0</identifier><identifier>PMID: 2443855</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino acids ; Analysis of the immune response. Humoral and cellular immunity ; Antigens - metabolism ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Computer Graphics ; Cytotoxicity, Immunologic ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; HLA Antigens - metabolism ; HLA-A2 Antigen ; Humans ; Immunity (Disease) ; Immunobiology ; Models, Molecular ; Organs and cells involved in the immune response ; Polymorphism, Genetic ; Protein Conformation ; Receptors, Immunologic - metabolism ; T-Lymphocytes - immunology ; T-Lymphocytes, Cytotoxic - immunology</subject><ispartof>Nature (London), 1987-10, Vol.329 (6139), p.512-518</ispartof><rights>1988 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Oct 8, 1987</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-3052ef419b286f4ac204c752841481a3ac60b0c0a090deac5a78b733003721913</citedby><cites>FETCH-LOGICAL-c427t-3052ef419b286f4ac204c752841481a3ac60b0c0a090deac5a78b733003721913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7514232$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2443855$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BJORKMAN, P. J</creatorcontrib><creatorcontrib>SAPER, M. A</creatorcontrib><creatorcontrib>SAMRAOUI, B</creatorcontrib><creatorcontrib>BENNETT, W. S</creatorcontrib><creatorcontrib>STROMINGER, J. L</creatorcontrib><creatorcontrib>WILEY, D. C</creatorcontrib><title>The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.</description><subject>Amino acids</subject><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Antigens - metabolism</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Computer Graphics</subject><subject>Cytotoxicity, Immunologic</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>HLA Antigens - metabolism</subject><subject>HLA-A2 Antigen</subject><subject>Humans</subject><subject>Immunity (Disease)</subject><subject>Immunobiology</subject><subject>Models, Molecular</subject><subject>Organs and cells involved in the immune response</subject><subject>Polymorphism, Genetic</subject><subject>Protein Conformation</subject><subject>Receptors, Immunologic - metabolism</subject><subject>T-Lymphocytes - immunology</subject><subject>T-Lymphocytes, Cytotoxic - immunology</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LAzEQhoMoWqvgHxCCiHhZnXxtkqMUPwqCl3pesml2jWyTmmwP_nsjVg9eepph3oeXmXkROiNwQ4CpW0a1INTAHpoQLuuK10ruowkAVRUoVh-h45zfAUAQyQ_RIeWcKSEmqFu8OdzF5HwfsAmj713ArQ9LH3qc_ejKcIkX2LphwMnZ2Ac_-hhK35eSceywHUzOeI7ffB6jjau1GX3rBz9-_jrmE3TQmSG7022doteH-8XsqXp-eZzP7p4ry6kcKwaCuo4T3VJVd9xYCtxKQRUnXBHDjK2hBQsGNCydscJI1UrGAJikRBM2RVc_vusUPzYuj83K5-_dTXBxkxtVvsWZVjtBVlMJWu12pIQoYLXcCRKuJaFaF_DiH_geNymUtzTlXA6a1aJA1z-QTTHn5LpmnfzKpM-GQPMdefMbeUHPt36bduWWf-A246JfbnWTrRm6ZIL1-Q-TgnDKKPsCDsKwRg</recordid><startdate>19871008</startdate><enddate>19871008</enddate><creator>BJORKMAN, P. J</creator><creator>SAPER, M. A</creator><creator>SAMRAOUI, B</creator><creator>BENNETT, W. S</creator><creator>STROMINGER, J. L</creator><creator>WILEY, D. C</creator><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>KL.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>19871008</creationdate><title>The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens</title><author>BJORKMAN, P. J ; SAPER, M. A ; SAMRAOUI, B ; BENNETT, W. S ; STROMINGER, J. L ; WILEY, D. C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-3052ef419b286f4ac204c752841481a3ac60b0c0a090deac5a78b733003721913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Amino acids</topic><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Antigens - metabolism</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Computer Graphics</topic><topic>Cytotoxicity, Immunologic</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>HLA Antigens - metabolism</topic><topic>HLA-A2 Antigen</topic><topic>Humans</topic><topic>Immunity (Disease)</topic><topic>Immunobiology</topic><topic>Models, Molecular</topic><topic>Organs and cells involved in the immune response</topic><topic>Polymorphism, Genetic</topic><topic>Protein Conformation</topic><topic>Receptors, Immunologic - metabolism</topic><topic>T-Lymphocytes - immunology</topic><topic>T-Lymphocytes, Cytotoxic - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BJORKMAN, P. J</creatorcontrib><creatorcontrib>SAPER, M. A</creatorcontrib><creatorcontrib>SAMRAOUI, B</creatorcontrib><creatorcontrib>BENNETT, W. S</creatorcontrib><creatorcontrib>STROMINGER, J. L</creatorcontrib><creatorcontrib>WILEY, D. C</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BJORKMAN, P. J</au><au>SAPER, M. A</au><au>SAMRAOUI, B</au><au>BENNETT, W. S</au><au>STROMINGER, J. L</au><au>WILEY, D. C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1987-10-08</date><risdate>1987</risdate><volume>329</volume><issue>6139</issue><spage>512</spage><epage>518</epage><pages>512-518</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>2443855</pmid><doi>10.1038/329512a0</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1987-10, Vol.329 (6139), p.512-518 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81034398 |
| source | MEDLINE; Nature; Springer Nature - Complete Springer Journals |
| subjects | Amino acids Analysis of the immune response. Humoral and cellular immunity Antigens - metabolism Binding Sites Biochemistry Biological and medical sciences Computer Graphics Cytotoxicity, Immunologic Epitopes Fundamental and applied biological sciences. Psychology Fundamental immunology HLA Antigens - metabolism HLA-A2 Antigen Humans Immunity (Disease) Immunobiology Models, Molecular Organs and cells involved in the immune response Polymorphism, Genetic Protein Conformation Receptors, Immunologic - metabolism T-Lymphocytes - immunology T-Lymphocytes, Cytotoxic - immunology |
| title | The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T23%3A47%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20foreign%20antigen%20binding%20site%20and%20T%20cell%20recognition%20regions%20of%20class%20I%20histocompatibility%20antigens&rft.jtitle=Nature%20(London)&rft.au=BJORKMAN,%20P.%20J&rft.date=1987-10-08&rft.volume=329&rft.issue=6139&rft.spage=512&rft.epage=518&rft.pages=512-518&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/329512a0&rft_dat=%3Cproquest_cross%3E21180367%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204409365&rft_id=info:pmid/2443855&rfr_iscdi=true |