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| {{STRUCTURE_2nw3| PDB=2nw3 | SCENE= }} | | {{STRUCTURE_2nw3| PDB=2nw3 | SCENE= }} |
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| '''Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''
| | ===Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17259989}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17259989 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17259989}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hla-b*3508]] | | [[Category: Hla-b*3508]] |
| [[Category: Mhc]] | | [[Category: Mhc]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:58:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:40:56 2008'' |