1u3h
From Proteopedia
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Crystal structure of mouse TCR 172.10 complexed with MHC class II I-Au molecule at 2.4 A
Overview
T cell receptor crossreactivity with different peptide ligands and biased, recognition of MHC are coupled features of antigen recognition that are, necessary for the T cell's diverse functional repertoire. In the crystal, structure between an autoreactive, EAE T cell clone 172.10 and myelin, basic protein (1-11) presented by class II MHC I-Au, recognition of the, MHC is dominated by the Vbeta domain of the TCR, which interacts with the, MHC alpha chain in a manner suggestive of a germline-encoded TCR/MHC, "anchor point." Strikingly, there are few specific contacts between the, TCR CDR3 loops and the MBP peptide. We also find that over 1,000,000, different peptides derived from combinatorial libraries can activate, 172.10, yet the TCR strongly prefers the native MBP contact residues. We, suggest that while TCR scanning of pMHC may be degenerate due to the TCR, germline bias for MHC, recognition of structurally distinct agonist, peptides is not indicative of TCR promiscuity, but rather highly specific, alternative solutions to TCR engagement.
About this Structure
1U3H is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity., Maynard J, Petersson K, Wilson DH, Adams EJ, Blondelle SE, Boulanger MJ, Wilson DB, Garcia KC, Immunity. 2005 Jan;22(1):81-92. PMID:15664161
Page seeded by OCA on Wed Nov 21 03:49:32 2007
