7TUG

Crystal structure of Tapasin in complex with PaSta2-Fab

7TUG の概要

• エントリーDOI: 10.2210/pdb7tug/pdb
• 関連するPDBエントリー: 7TUC 7TUD 7TUE 7TUF 7TUH
• 分子名称: Tapasin, PaSta2 Fab heavy chain, PaSta2 Fab kappa light chain, ... (4 entities in total)
• 機能のキーワード: pasta, fab, antibody, igg, mhc-i, hla, peptide loading complex, plc, antigen presentation, immune response, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 94032.52

構造登録者

Jiang, J.,Natarajan, K.,Taylor, D.K.,Boyd, L.F.,Margulies, D.H. (登録日: 2022-02-02, 公開日: 2022-09-07, 最終更新日: 2024-11-13)

主引用文献

Jiang, J.,Taylor, D.K.,Kim, E.J.,Boyd, L.F.,Ahmad, J.,Mage, M.G.,Truong, H.V.,Woodward, C.H.,Sgourakis, N.G.,Cresswell, P.,Margulies, D.H.,Natarajan, K.
Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.
Nat Commun, 13:5470-5470, 2022

PubMed Abstract: Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide loading complex plays a critical role in antigen presentation and immune recognition. Mechanistic insight has been hampered by the lack of detailed structural information concerning tapasin-MHC-I. We present here crystal structures of human tapasin complexed with the MHC-I molecule HLA-B*44:05, and with each of two anti-tapasin antibodies. The tapasin-stabilized peptide-receptive state of HLA-B*44:05 is characterized by distortion of the peptide binding groove and destabilization of the β-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and β-microglobulin accompany the transition to a peptide-receptive state. Together this ensemble of crystal structures provides insights into a distinct mechanism of tapasin-mediated peptide exchange.

PubMed: 36115831
DOI: 10.1038/s41467-022-33153-8

実験手法

X-RAY DIFFRACTION (3.9 Å)