1IM9

Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1 bound to its MHC ligand HLA-Cw4

1IM9 の概要

• エントリーDOI: 10.2210/pdb1im9/pdb
• 関連するPDBエントリー: 1NKR 1QQD
• 分子名称: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, CW-4 CW*0401 ALPHA CHAIN, Beta-2 microglobulin, HLA-Cw4-specific peptide, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, immunoglobulin domain, antiparallel beta sheet, alpha helix, 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; Cell membrane; Single-pass type I membrane protein: P43626
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 115057.53

構造登録者

Fan, Q.R.,Long, E.O.,Wiley, D.C. (登録日: 2001-05-10, 公開日: 2001-05-30, 最終更新日: 2024-10-30)

主引用文献

Fan, Q.R.,Long, E.O.,Wiley, D.C.
Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex.
Nat.Immunol., 2:452-460, 2001

PubMed Abstract: Inhibitory natural killer (NK) cell receptors down-regulate the cytotoxicity of NK cells upon recognition of specific class I major histocompatibility complex (MHC) molecules on target cells. We report here the crystal structure of the inhibitory human killer cell immunoglobulin-like receptor 2DL1 (KIR2DL1) bound to its class I MHC ligand, HLA-Cw4. The KIR2DL1-HLA-Cw4 interface exhibits charge and shape complementarity. Specificity is mediated by a pocket in KIR2DL1 that hosts the Lys80 residue of HLA-Cw4. Many residues conserved in HLA-C and in KIR2DL receptors make different interactions in KIR2DL1-HLA-Cw4 and in a previously reported KIR2DL2-HLA-Cw3 complex. A dimeric aggregate of KIR-HLA-C complexes was observed in one KIR2DL1-HLA-Cw4 crystal. Most of the amino acids that differ between human and chimpanzee KIRs with HLA-C specificities form solvent-accessible clusters outside the KIR-HLA interface, which suggests undiscovered interactions by KIRs.

PubMed: 11323700

実験手法

X-RAY DIFFRACTION (2.8 Å)