1I3R

CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE

1I3R の概要

• エントリーDOI: 10.2210/pdb1i3r/pdb
• 関連するPDBエントリー: 1IEA 1IEB
• 分子名称: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, E-K ALPHA CHAIN, FUSION PROTEIN CONSISTING OF MHC E-BETA-K PRECURSOR, GLYCINE RICH LINKER, AND HEMOGLOBIN BETA-2 CHAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: mhc classii, immune system
• 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 : P04224
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 196474.92

構造登録者

Kappler, J.W.,Wilson, N. (登録日: 2001-02-15, 公開日: 2001-06-20, 最終更新日: 2024-10-30)

主引用文献

Wilson, N.,Fremont, D.,Marrack, P.,Kappler, J.
Mutations changing the kinetics of class II MHC peptide exchange.
Immunity, 14:513-522, 2001

PubMed Abstract: IE/DR MHC class II molecules have an extensive H-bonding network under the bound peptide. In IE(k), two alpha chain acidic amino acids in the core of this network were mutated to amides. At low pH, the mutant molecule exchanged peptide much more rapidly than the wild-type. The crystal structure of the mutant IE(k) revealed the loss of a single buried water molecule and a reorganization of the predicted H-bonding network. We suggest that these mutations enhance the transition of MHC class II to an open conformation at low pH allowing the bound peptide to escape. In wild-type IE(k), the need to protonate these amino acids also may be a bottleneck in the return to a closed conformation after peptide binding.

PubMed: 11371354
DOI: 10.1016/S1074-7613(01)00140-6

実験手法

X-RAY DIFFRACTION (2.4 Å)