5OPI

Crystal structure of the TAPBPR-MHC I peptide editing complex

5OPI の概要

• エントリーDOI: 10.2210/pdb5opi/pdb
• 分子名称: H-2 class I histocompatibility antigen, D-B alpha chain, Beta-2-microglobulin, TAP binding protein-like variant (3 entities in total)
• 機能のキーワード: adaptive immunity, antigen processing, antigen presentation, peptide proofreading, 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: P01899; Secreted . Note=(Microbial infection) In the presence of M: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 83779.87

構造登録者

Thomas, C.,Tampe, R. (登録日: 2017-08-09, 公開日: 2017-10-18, 最終更新日: 2024-11-06)

主引用文献

Thomas, C.,Tampe, R.
Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.
Science, 358:1060-1064, 2017

PubMed Abstract: Adaptive immunity is shaped by a selection of peptides presented on major histocompatibility complex class I (MHC I) molecules. The chaperones Tapasin (Tsn) and TAP-binding protein-related (TAPBPR) facilitate MHC I peptide loading and high-affinity epitope selection. Despite the pivotal role of Tsn and TAPBPR in controlling the hierarchical immune response, their catalytic mechanism remains unknown. Here, we present the x-ray structure of the TAPBPR-MHC I complex, which delineates the central step of catalysis. TAPBPR functions as peptide selector by remodeling the MHC I α2-1-helix region, stabilizing the empty binding groove, and inserting a loop into the groove that interferes with peptide binding. The complex explains how mutations in MHC I-specific chaperones cause defects in antigen processing and suggests a unifying mechanism of peptide proofreading.

PubMed: 29025996
DOI: 10.1126/science.aao6001

実験手法

X-RAY DIFFRACTION (3.3 Å)