3IXA

Human Class I MHC HLA-A2(A150P) in complex with the Tax peptide

3IXA の概要

• エントリーDOI: 10.2210/pdb3ixa/pdb
• 関連するPDBエントリー: 1DUZ 3H9H
• 分子名称: HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Tax peptide, ... (5 entities in total)
• 機能のキーワード: tel1p, tax, a150p mutation, nonapeptide, mhc class i, hla-a2, tcr a6, cross-reactivity, disulfide bond, glycoprotein, host-virus interaction, immune response, membrane, mhc i, phosphoprotein, transmembrane, disease mutation, glycation, immunoglobulin domain, pyrrolidone carboxylic acid, secreted, 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 . Note=(Microbial infection) In the presence of M: P61769
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 90028.12

構造登録者

Borbulevych, O.Y.,Baker, B.M. (登録日: 2009-09-03, 公開日: 2010-01-12, 最終更新日: 2023-09-06)

主引用文献

Borbulevych, O.Y.,Piepenbrink, K.H.,Gloor, B.E.,Scott, D.R.,Sommese, R.F.,Cole, D.K.,Sewell, A.K.,Baker, B.M.
T cell receptor cross-reactivity directed by antigen-dependent tuning of peptide-MHC molecular flexibility.
Immunity, 31:885-896, 2009

PubMed Abstract: T cell-mediated immunity requires T cell receptor (TCR) cross-reactivity, the mechanisms behind which remain incompletely elucidated. The alphabeta TCR A6 recognizes both the Tax (LLFGYPVYV) and Tel1p (MLWGYLQYV) peptides presented by the human class I MHC molecule HLA-A2. Here we found that although the two ligands are ideal structural mimics, they form substantially different interfaces with A6, with conformational differences in the peptide, the TCR, and unexpectedly, the MHC molecule. The differences between the Tax and Tel1p ternary complexes could not be predicted from the free peptide-MHC structures and are inconsistent with a traditional induced-fit mechanism. Instead, the differences were attributable to peptide and MHC molecular motion present in Tel1p-HLA-A2 but absent in Tax-HLA-A2. Differential "tuning" of the dynamic properties of HLA-A2 by the Tax and Tel1p peptides thus facilitates cross-recognition and impacts how structural diversity can be presented to and accommodated by receptors of the immune system.

PubMed: 20064447
DOI: 10.1016/j.immuni.2009.11.003

実験手法

X-RAY DIFFRACTION (2.1 Å)