1QSE

STRUCTURE OF HUMAN A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE V7R

1QSE の概要

• エントリーDOI: 10.2210/pdb1qse/pdb
• 関連するPDBエントリー: 1AO7 1BD2
• 分子名称: PROTEIN (MHC class I HLA-A), PROTEIN (beta-2 microglobulin), Tax Peptide V7R, ... (5 entities in total)
• 機能のキーワード: human t cell receptor, tcr-peptide-mhc complex, hla-a2, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 93996.15

構造登録者

Ding, Y.H.,Baker, B.M.,Garboczi, D.N.,Biddison, W.E.,Wiley, D.C. (登録日: 1999-06-21, 公開日: 1999-12-21, 最終更新日: 2024-11-13)

主引用文献

Ding, Y.H.,Baker, B.M.,Garboczi, D.N.,Biddison, W.E.,Wiley, D.C.
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical.
Immunity, 11:45-56, 1999

PubMed Abstract: 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.

PubMed: 10435578
DOI: 10.1016/S1074-7613(00)80080-1

実験手法

X-RAY DIFFRACTION (2.8 Å)