2ol3: Difference between revisions

Revision as of 15:38, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ol3.png

Template:STRUCTURE 2ol3

crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I moleculecrystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule

Template:ABSTRACT PUBMED 17363906

About this StructureAbout this Structure

2OL3 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?, Mazza C, Auphan-Anezin N, Gregoire C, Guimezanes A, Kellenberger C, Roussel A, Kearney A, van der Merwe PA, Schmitt-Verhulst AM, Malissen B, EMBO J. 2007 Apr 4;26(7):1972-83. Epub 2007 Mar 15. PMID:17363906

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OCA

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-[[Image:2ol3.gif|left|200px]]
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 {{STRUCTURE_2ol3|  PDB=2ol3  |  SCENE=  }}
-'''crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule'''
+===crystal structure of BM3.3 ScFV TCR in complex with PBM8-H-2KBM8 MHC class I molecule===
-==Overview==
+<!--
-Binding degeneracy is thought to constitute a fundamental property of the T-cell antigen receptor (TCR), yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and a peptide (pBM8) bound to the H-2K(bm8) major histocompatibility complex (MHC) molecule, and compared it with the structures of the BM3.3 TCR bound to H-2K(b) molecules loaded with two peptides that had a minimal level of primary sequence identity with pBM8. Our findings provide a refined structural view of the basis of BM3.3 TCR cross-reactivity and a structural explanation for the long-standing paradox that a TCR antigen-binding site can be both specific and degenerate. We also measured the thermodynamic features and biological penalties that incurred during cross-recognition. Our data illustrate the difficulty for a given TCR in adapting to distinct peptide-MHC surfaces while still maintaining affinities that result in functional in vivo responses. Therefore, when induction of protective effector T cells is used as the ultimate criteria for adaptive immunity, TCRs are probably much less degenerate than initially assumed.
+The line below this paragraph, {{ABSTRACT_PUBMED_17363906}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: T cell receptor]]
 [[Category: Tcr-pmhc complex]]
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