1FYT

CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1

1FYT の概要

• エントリーDOI: 10.2210/pdb1fyt/pdb
• 関連するPDBエントリー: 1DLH
• 分子名称: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN, HEMAGGLUTININ HA1 PEPTIDE CHAIN, ... (7 entities in total)
• 機能のキーワード: protein-protein complex, immunoglobulin fold, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 96710.28

構造登録者

Hennecke, J.,Carfi, A.,Wiley, D.C. (登録日: 2000-10-03, 公開日: 2000-11-08, 最終更新日: 2024-10-30)

主引用文献

Hennecke, J.,Carfi, A.,Wiley, D.C.
Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1.
EMBO J., 19:5611-5624, 2000

PubMed Abstract: An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA) peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to increase the local concentration of the interacting proteins once the peptide has been loaded onto the major histocompatibility complex (MHC) molecule. The structure of the complex, determined by X-ray crystallography, has a binding mode similar to that of the human B7 alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted are at the same positions observed earlier in class I MHC/peptide/TCR complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the response to HA/HLA-DR appears to conserve charged interactions between three lysines of the peptide and acidic residues on the TCR.

PubMed: 11060013
DOI: 10.1093/emboj/19.21.5611

実験手法

X-RAY DIFFRACTION (2.6 Å)