9OCI

Transporter associated with antigen processing (TAP) bound to the viral protein rhUS6 in the outward-facing open state

9OCI の概要

• エントリーDOI: 10.2210/pdb9oci/pdb
• EMDBエントリー: 70316
• 分子名称: Antigen peptide transporter 2, TAP transport inhibitor rhUS6, Antigen peptide transporter 1, ... (6 entities in total)
• 機能のキーワード: abc transporter, antigen processing, peptide transporter, membrane protein, immune evasion, cytomegalovirus, herpesvirus
• 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: 196972.81

構造登録者

Lee, J.,Manon, V.,Chen, J. (登録日: 2025-04-24, 公開日: 2025-09-10, 最終更新日: 2026-03-18)

主引用文献

Lee, J.,Manon, V.,Chen, J.
Structurally diverse viral inhibitors converge on a shared mechanism to stall the antigen transporter TAP.
Proc.Natl.Acad.Sci.USA, 122:e2516676122-e2516676122, 2025

PubMed Abstract: In the host-pathogen arms race, herpesviruses and poxviruses encode proteins that sabotage the transporter associated with antigen processing (TAP), thereby suppressing MHC-I antigen presentation and enabling lifelong infection. Of the five known viral TAP inhibitors, only the herpes simplex virus (HSV) protein ICP47 has been structurally resolved. We now report cryoelectron microscopy structures of TAP in complex with the remaining four: BNLF2a (Epstein-Barr virus), hUS6 (human cytomegalovirus), bUL49.5 (bovine herpesvirus 1), and CPXV012 (cowpox virus), assembling a structural atlas of viral TAP evasion. Despite employing divergent sequences, folds, and conformational targets, these viral inhibitors converge on a common strategy: they stall TAP from the alternating access cycle, precluding peptide entry into the ER and shielding infected cells from cytotoxic T cell surveillance. These findings reveal striking functional convergence and provide a structural framework for rational antiviral design.

PubMed: 40956880
DOI: 10.1073/pnas.2516676122

実験手法

ELECTRON MICROSCOPY (3.3 Å)