3VXR

The complex between H27-14 TCR and HLA-A24 bound to HIV-1 Nef134-10(wt) peptide

3VXR の概要

• エントリーDOI: 10.2210/pdb3vxr/pdb
• 関連するPDBエントリー: 3VXM 3VXN 3VXO 3VXP 3VXQ 3VXS 3VXT 3VXU
• 分子名称: HLA class I histocompatibility antigen, A-24 alpha chain, Beta-2-microglobulin, H27-14 TCR alpha chain, ... (6 entities in total)
• 機能のキーワード: hiv-1, nef, immune system, hla-a24, t cell receptor, mhc class i, immunogloburin domain, tcr, mhc, immune response
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05534; Secreted: P61769
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 95584.21

構造登録者

Shimizu, A.,Fukai, S.,Yamagata, A.,Iwamoto, A. (登録日: 2012-09-20, 公開日: 2013-10-23, 最終更新日: 2024-11-20)

主引用文献

Shimizu, A.,Kawana-Tachikawa, A.,Yamagata, A.,Han, C.,Zhu, D.,Sato, Y.,Nakamura, H.,Koibuchi, T.,Carlson, J.,Martin, E.,Brumme, C.J.,Shi, Y.,Gao, G.F.,Brumme, Z.L.,Fukai, S.,Iwamoto, A.
Structure of TCR and antigen complexes at an immunodominant CTL epitope in HIV-1 infection
SCI REP, 3:3097-3097, 2013

PubMed Abstract: We investigated the crystal structure of an HLA-A*2402-restricted CTL epitope in the HIV-1 nef gene (Nef134-10) before (pHLA) or after TCR docking. The wild type epitope and two escape mutants were included in the study. Y135F was an early-appearing major mutation, while F139L was a late-appearing mutation which was selected in the patients without Y135F. F139 was an eminent feature of the Nef134-10 epitope. Wild type-specific TCR was less fit to F139L mutant suggesting that F139L is an escape from the CTL against the wild type epitope. Although Y135F mutation disrupted the hydrogen bond to HLA-A*2402 His70, newly formed hydrogen bond between T138 and His70 kept the conformation of the epitope in the reconstituted pMHC. TCR from Y135F- or dually-specific CTL had unique mode of binding to the mutant epitope. Y135F has been reported as a processing mutant but CTL carrying structurally adequate TCR can be found in the patients.

PubMed: 24192765
DOI: 10.1038/srep03097

実験手法

X-RAY DIFFRACTION (2.4 Å)