5WEU

Crystal Structure of H2-Dd with disulfide-linked 10mer peptide

5WEU の概要

• エントリーDOI: 10.2210/pdb5weu/pdb
• 関連するPDBエントリー: 5WER 5WES 5WET
• 分子名称: H-2 class I histocompatibility antigen, D-D alpha chain, Beta-2-microglobulin, Envelope glycoprotein gp160, ... (5 entities in total)
• 機能のキーワード: antigen presentation, peptide editing, major histompatibility complex class i, mhc-i, tapbpr, h2-dd, h-2dd, tapasin, peptide loading complex, plc, immune response, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01900; Secreted: P01887; Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P03377
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45335.94

構造登録者

Jiang, J.S.,Natarajan, K.,Boyd, L.F.,Margulies, D.H. (登録日: 2017-07-10, 公開日: 2017-10-18, 最終更新日: 2024-10-09)

主引用文献

Jiang, J.,Natarajan, K.,Boyd, L.F.,Morozov, G.I.,Mage, M.G.,Margulies, D.H.
Crystal structure of a TAPBPR-MHC I complex reveals the mechanism of peptide editing in antigen presentation.
Science, 358:1064-1068, 2017

PubMed Abstract: Central to CD8 T cell-mediated immunity is the recognition of peptide-major histocompatibility complex class I (p-MHC I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC I is a key step in the MHC I antigen presentation pathway. However, the structure of MHC I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC I in complex with the peptide editor TAPBPR (TAP-binding protein-related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin.

PubMed: 29025991
DOI: 10.1126/science.aao5154

実験手法

X-RAY DIFFRACTION (1.584 Å)