1U3H

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

1U3H の概要

• エントリーDOI: 10.2210/pdb1u3h/pdb
• 関連するPDBエントリー: 1k2d
• 分子名称: 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)
• 機能のキーワード: complex, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 137726.78

構造登録者

Maynard, J.,Petersson, K.,Wilson, D.H.,Adams, E.J.,Blondelle, S.E.,Boulanger, M.J.,Wilson, D.B.,Garcia, K.C. (登録日: 2004-07-21, 公開日: 2005-05-17, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.42 Å)