1HSA

THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC

1HSA の概要

• エントリーDOI: 10.2210/pdb1hsa/pdb
• 分子名称: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-B*2705), BETA 2-MICROGLOBULIN, MODEL PEPTIDE SEQUENCE - ARAAAAAAA, ... (4 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: P03989; Secreted: P61769
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 88840.30

構造登録者

Madden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C. (登録日: 1992-08-11, 公開日: 1992-10-15, 最終更新日: 2024-10-23)

主引用文献

Madden, D.R.,Gorga, J.C.,Strominger, J.L.,Wiley, D.C.
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC.
Cell(Cambridge,Mass.), 70:1035-1048, 1992

PubMed Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.

PubMed: 1525820
DOI: 10.1016/0092-8674(92)90252-8

実験手法

X-RAY DIFFRACTION (2.1 Å)