1R5V

Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation

1R5V の概要

• エントリーDOI: 10.2210/pdb1r5v/pdb
• 分子名称: H-2 class II histocompatibility antigen, E-K alpha chain, artificial peptide, MHC H2-IE-beta, ... (4 entities in total)
• 機能のキーワード: tcr, mhc class ii, structural rearangement, signaling protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): P04224 P18468
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 88220.47

構造登録者

Krogsgaard, M.,Prado, N.,Adams, E.J.,He, X.L.,Chow, D.C.,Wilson, D.B.,Garcia, K.C.,Davis, M.M. (登録日: 2003-10-13, 公開日: 2004-02-03, 最終更新日: 2024-10-16)

主引用文献

Krogsgaard, M.,Prado, N.,Adams, E.J.,He, X.L.,Chow, D.C.,Wilson, D.B.,Garcia, K.C.,Davis, M.M.
Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation.
Mol.Cell, 12:1367-1378, 2003

PubMed Abstract: While in many cases the half-life of T cell receptor (TCR) binding to a particular ligand is a good predictor of activation potential, numerous exceptions suggest that other physical parameter(s) must also play a role. Accordingly, we analyzed the thermodynamics of TCR binding to a series of peptide-MHC ligands, three of which are more stimulatory than their stability of binding would predict. Strikingly, we find that during TCR binding these outliers show anomalously large changes in heat capacity, an indicator of conformational change or flexibility in a binding interaction. By combining the values for heat capacity (DeltaCp) and the half-life of TCR binding (t(1/2)), we find that we can accurately predict the degree of T cell stimulation. Structural analysis shows significant changes in the central TCR contact residue of the peptide-MHC, indicating that structural rearrangements within the TCR-peptide-MHC interface can contribute to T cell activation.

PubMed: 14690592
DOI: 10.1016/S1097-2765(03)00474-X

実験手法

X-RAY DIFFRACTION (2.5 Å)