A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)–restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide–MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non...
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| Veröffentlicht in: | Nature Immunology 2007-03, Vol.8 (3), p.268-276 |
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| creator | Tynan, Fleur E Reid, Hugh H Kjer-Nielsen, Lars Miles, John J Wilce, Matthew C J Kostenko, Lyudmila Borg, Natalie A Williamson, Nicholas A Beddoe, Travis Purcell, Anthony W Burrows, Scott R McCluskey, James Rossjohn, Jamie |
| description | Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)–restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide–MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B
*
3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide. |
| doi_str_mv | 10.1038/ni1432 |
| format | Article |
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*
3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.</description><identifier>ISSN: 1529-2908</identifier><identifier>EISSN: 1529-2916</identifier><identifier>EISSN: 1365-2567</identifier><identifier>DOI: 10.1038/ni1432</identifier><identifier>PMID: 17259989</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Animals ; Antigen Presentation - immunology ; Antigens, Viral - chemistry ; Antigens, Viral - immunology ; Biomedical and Life Sciences ; Biomedicine ; Cell receptors ; Epitopes, T-Lymphocyte - chemistry ; Epitopes, T-Lymphocyte - immunology ; Epstein-Barr virus ; Flow Cytometry ; Histocompatibility Antigens Class I - chemistry ; Histocompatibility Antigens Class I - immunology ; Humans ; Immune recognition ; Immunology ; Infectious Diseases ; Major histocompatibility complex ; Physiological aspects ; Plasticity ; Protein Structure, Quaternary ; Receptors, Antigen, T-Cell - chemistry ; Receptors, Antigen, T-Cell - immunology ; T cells</subject><ispartof>Nature Immunology, 2007-03, Vol.8 (3), p.268-276</ispartof><rights>Springer Nature America, Inc. 2007</rights><rights>COPYRIGHT 2007 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Mar 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-748e9b65b1c205c38947888829324487e81bd315e02d6f25d2830f57df451b073</citedby><cites>FETCH-LOGICAL-c500t-748e9b65b1c205c38947888829324487e81bd315e02d6f25d2830f57df451b073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ni1432$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ni1432$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17259989$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tynan, Fleur E</creatorcontrib><creatorcontrib>Reid, Hugh H</creatorcontrib><creatorcontrib>Kjer-Nielsen, Lars</creatorcontrib><creatorcontrib>Miles, John J</creatorcontrib><creatorcontrib>Wilce, Matthew C J</creatorcontrib><creatorcontrib>Kostenko, Lyudmila</creatorcontrib><creatorcontrib>Borg, Natalie A</creatorcontrib><creatorcontrib>Williamson, Nicholas A</creatorcontrib><creatorcontrib>Beddoe, Travis</creatorcontrib><creatorcontrib>Purcell, Anthony W</creatorcontrib><creatorcontrib>Burrows, Scott R</creatorcontrib><creatorcontrib>McCluskey, James</creatorcontrib><creatorcontrib>Rossjohn, Jamie</creatorcontrib><title>A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule</title><title>Nature Immunology</title><addtitle>Nat Immunol</addtitle><addtitle>Nat Immunol</addtitle><description>Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)–restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide–MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B
*
3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.</description><subject>Animals</subject><subject>Antigen Presentation - immunology</subject><subject>Antigens, Viral - chemistry</subject><subject>Antigens, Viral - immunology</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell receptors</subject><subject>Epitopes, T-Lymphocyte - chemistry</subject><subject>Epitopes, T-Lymphocyte - immunology</subject><subject>Epstein-Barr virus</subject><subject>Flow Cytometry</subject><subject>Histocompatibility Antigens Class I - chemistry</subject><subject>Histocompatibility Antigens Class I - immunology</subject><subject>Humans</subject><subject>Immune recognition</subject><subject>Immunology</subject><subject>Infectious Diseases</subject><subject>Major histocompatibility complex</subject><subject>Physiological aspects</subject><subject>Plasticity</subject><subject>Protein Structure, Quaternary</subject><subject>Receptors, Antigen, T-Cell - 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Academic</collection><jtitle>Nature Immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tynan, Fleur E</au><au>Reid, Hugh H</au><au>Kjer-Nielsen, Lars</au><au>Miles, John J</au><au>Wilce, Matthew C J</au><au>Kostenko, Lyudmila</au><au>Borg, Natalie A</au><au>Williamson, Nicholas A</au><au>Beddoe, Travis</au><au>Purcell, Anthony W</au><au>Burrows, Scott R</au><au>McCluskey, James</au><au>Rossjohn, Jamie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule</atitle><jtitle>Nature Immunology</jtitle><stitle>Nat Immunol</stitle><addtitle>Nat Immunol</addtitle><date>2007-03-01</date><risdate>2007</risdate><volume>8</volume><issue>3</issue><spage>268</spage><epage>276</epage><pages>268-276</pages><issn>1529-2908</issn><eissn>1529-2916</eissn><eissn>1365-2567</eissn><abstract>Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)–restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide–MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B
*
3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>17259989</pmid><doi>10.1038/ni1432</doi><tpages>9</tpages></addata></record> |
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| subjects | Animals Antigen Presentation - immunology Antigens, Viral - chemistry Antigens, Viral - immunology Biomedical and Life Sciences Biomedicine Cell receptors Epitopes, T-Lymphocyte - chemistry Epitopes, T-Lymphocyte - immunology Epstein-Barr virus Flow Cytometry Histocompatibility Antigens Class I - chemistry Histocompatibility Antigens Class I - immunology Humans Immune recognition Immunology Infectious Diseases Major histocompatibility complex Physiological aspects Plasticity Protein Structure, Quaternary Receptors, Antigen, T-Cell - chemistry Receptors, Antigen, T-Cell - immunology T cells |
| title | A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule |
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