2ol3: Difference between revisions

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[[Image:2ol3.gif|left|200px]]
{{Seed}}
[[Image:2ol3.png|left|200px]]


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{{STRUCTURE_2ol3|  PDB=2ol3  |  SCENE=  }}  
{{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==
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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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{{ABSTRACT_PUBMED_17363906}}


==About this Structure==
==About this Structure==
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[[Category: T cell receptor]]
[[Category: T cell receptor]]
[[Category: Tcr-pmhc complex]]
[[Category: Tcr-pmhc complex]]
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