1qrn
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A
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Overview
The interactions of three singly substituted peptide variants of the, HTLV-1 Tax peptide bound to HLA-A2 with the A6 T cell receptor have been, studied using T cell assays, kinetic and thermodynamic measurements, and, X-ray crystallography. The three peptide/MHC ligands include weak agonists, and antagonists with different affinities for TCR. The three-dimensional, structures of the three A6-TCR/peptide/HLA-A2 complexes are remarkably, similar to each other and to the wild-type agonist complex, with minor, adjustments at the interface to accommodate the peptide substitutions, (P6A, V7R, and Y8A). The lack of correlation between structural changes, and the type of T cell signals induced provides direct evidence that, different signals are not generated by different ligand-induced, conformational changes in the alphabeta TCR.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this Structure
1QRN is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical., Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC, Immunity. 1999 Jul;11(1):45-56. PMID:10435578
Page seeded by OCA on Mon Nov 12 18:55:58 2007
