1HHH

THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A2

1HHH の概要

• エントリーDOI: 10.2210/pdb1hhh/pdb
• 分子名称: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A*0201) (ALPHA CHAIN), BETA 2-MICROGLOBULIN, HEPATITIS B NUCLEOCAPSID PROTEIN (RESIDUES 18-27) (3 entities in total)
• 機能のキーワード: histocompatibility antigen
• 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: P01892; Secreted: P61769; Capsid protein: Virion: P12901
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44888.86

構造登録者

Madden, D.R.,Garboczi, D.N.,Wiley, D.C. (登録日: 1993-06-30, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Madden, D.R.,Garboczi, D.N.,Wiley, D.C.
The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2.
Cell(Cambridge,Mass.), 75:693-708, 1993

PubMed Abstract: Complexes of five peptides (from HIV-1, influenza A virus, HTLV-1, and hepatitis B virus proteins) bound to the human class I MHC molecule HLA-A2 have been studied by X-ray crystallography. While the peptide termini and their second and C-terminal anchor side chains are bound similarly in all five cases, the main chain and side chain conformations of each peptide are strikingly different in the center of the binding site, and these differences are accessible to direct TCR recognition. Each of the central peptide residues is seen to point up for some bound peptides, but down or sideways for others. Thus, although fixed at its ends, the structure of an MHC-bound peptide appears to be a highly complex function of its entire sequence, potentially sensitive to even small sequence differences. In contrast, MHC structural variation is relatively limited. These results offer a structural framework for understanding the role of nonanchor peptide side chains in both peptide-MHC binding affinity and TCR recognition.

PubMed: 7694806
DOI: 10.1016/0092-8674(93)90490-H

実験手法

X-RAY DIFFRACTION (3 Å)