1U3H

Crystal structure of mouse TCR 172.10 complexed with MHC class II I-Au molecule at 2.4 A

Summary for 1U3H

• Entry DOI: 10.2210/pdb1u3h/pdb
• Related: 1k2d
• Descriptor: T-cell receptor alpha-chain, Mouse TCRVbeta 172.10, extracellular variable domain, H-2 class II histocompatibility antigen, A-U alpha chain, ... (6 entities in total)
• Functional Keywords: complex, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 10
• Total formula weight: 137726.78

Authors

Maynard, J.,Petersson, K.,Wilson, D.H.,Adams, E.J.,Blondelle, S.E.,Boulanger, M.J.,Wilson, D.B.,Garcia, K.C. (deposition date: 2004-07-21, release date: 2005-05-17, Last modification date: 2024-10-30)

Primary citation

Maynard, J.,Petersson, K.,Wilson, D.H.,Adams, E.J.,Blondelle, S.E.,Boulanger, M.J.,Wilson, D.B.,Garcia, K.C.
Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity
Immunity, 22:81-92, 2005

PubMed Abstract: 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.

PubMed: 15664161
DOI: 10.1016/j.immuni.2004.11.015

Experimental method

X-RAY DIFFRACTION (2.42 Å)