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1HHJ

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

1HHJ の概要
エントリーDOI10.2210/pdb1hhj/pdb
分子名称CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A*0201) (ALPHA CHAIN), BETA 2-MICROGLOBULIN, HIV-1 REVERSE TRANSCRIPTASE (RESIDUES 309-317) (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
Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P04588
タンパク質・核酸の鎖数6
化学式量合計89453.52
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: 2024-11-06)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1hhj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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