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| {{STRUCTURE_1kb5| PDB=1kb5 | SCENE= }} | | {{STRUCTURE_1kb5| PDB=1kb5 | SCENE= }} |
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| '''MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX'''
| | ===MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX=== |
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| ==Overview==
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| The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment complexed to the Fab fragment of a specific anti-clonotypic antibody has been determined to 2.6 A resolution. The polypeptide backbone of the TCR V alpha domain is very similar to those of other crystallographically determined V alphas, whereas the V beta structure is so far unique among TCR V beta domains in that it displays a switch of the c" strand from the inner to the outer beta-sheet. The beta chain variable region of this TCR antigen-binding site is characterized by a rather elongated third complementarity-determining region (CDR3beta) that packs tightly against the CDR3 loop of the alpha chain, without leaving any intervening hydrophobic pocket. Thus, the conformation of the CDR loops with the highest potential diversity distinguishes the structure of this TCR antigen-binding site from those for which crystallographic data are available. On the basis of all these results, we infer that a significant conformational change of the CDR3beta loop found in our TCR is required for binding to its cognate peptide-MHC ligand.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9250664}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9250664 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9250664}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Strand switch]] | | [[Category: Strand switch]] |
| [[Category: T-cell receptor]] | | [[Category: T-cell receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:31:38 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:04:00 2008'' |
