1QQD

CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR

1QQD の概要

• エントリーDOI: 10.2210/pdb1qqd/pdb
• 分子名称: HISTOCOMPATIBILITY LEUKOCYTE ANTIGEN (HLA)-CW4 (HEAVY CHAIN), BETA-2 MICROGLOBULIN, HLA-CW4 SPECIFIC PEPTIDE, ... (4 entities in total)
• 機能のキーワード: immunoglobulin (ig)-like domain, alpha helix, beta sheet, immune system
• 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: P30504; Secreted: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44622.19

構造登録者

Fan, Q.R.,Wiley, D.C. (登録日: 1999-06-03, 公開日: 1999-12-08, 最終更新日: 2024-11-20)

主引用文献

Fan, Q.R.,Wiley, D.C.
Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor
J.Exp.Med., 190:113-123, 1999

PubMed Abstract: The crystal structure of the human class I major histocompatibility complex molecule, human histocompatibility leukocyte antigen (HLA)-Cw4, the ligand for a natural killer (NK) cell inhibitory receptor, has been determined, complexed with a nonameric consensus peptide (QYDDAVYKL). Relative to HLA-A2, the peptide binding groove is widened around the COOH terminus of the alpha 1 helix, which contains residues that determine the specificity of HLA-Cw4 for the inhibitory NK receptor, KIR2D. The structure reveals an unusual pattern of internal hydrogen bonding among peptide residues. The peptide is anchored in four specificity pockets in the cleft and secured by extensive hydrogen bonds between the peptide main chain and the cleft. The surface of HLA-Cw4 has electrostatic complementarity to the surface of the NK cell inhibitory receptor KIR2D.

PubMed: 10429675
DOI: 10.1084/jem.190.1.113

実験手法

X-RAY DIFFRACTION (2.7 Å)