3QXA

HLA-DR1 bound with CLIP peptide

3QXA の概要

• エントリーDOI: 10.2210/pdb3qxa/pdb
• 関連するPDBエントリー: 3QXD
• 分子名称: HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-1 beta chain, HLA class II histocompatibility antigen gamma chain peptide, ... (4 entities in total)
• 機能のキーワード: mhc class ii, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P01903 P04229; Cell membrane; Single-pass type II membrane protein (Potential): P04233
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 89825.37

構造登録者

Painter, C.A.,Stern, L.J. (登録日: 2011-03-01, 公開日: 2011-11-16, 最終更新日: 2024-10-30)

主引用文献

Painter, C.A.,Negroni, M.P.,Kellersberger, K.A.,Zavala-Ruiz, Z.,Evans, J.E.,Stern, L.J.
Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange.
Proc.Natl.Acad.Sci.USA, 108:19329-19334, 2011

PubMed Abstract: HLA-DM is required for efficient peptide exchange on class II MHC molecules, but its mechanism of action is controversial. We trapped an intermediate state of class II MHC HLA-DR1 by substitution of αF54, resulting in a protein with increased HLA-DM binding affinity, weakened MHC-peptide hydrogen bonding as measured by hydrogen-deuterium exchange mass spectrometry, and increased susceptibility to DM-mediated peptide exchange. Structural analysis revealed a set of concerted conformational alterations at the N-terminal end of the peptide-binding site. These results suggest that interaction with HLA-DM is driven by a conformational change of the MHC II protein in the region of the α-subunit 3(10) helix and adjacent extended strand region, and provide a model for the mechanism of DM-mediated peptide exchange.

PubMed: 22084083
DOI: 10.1073/pnas.1108074108

実験手法

X-RAY DIFFRACTION (2.712 Å)