1IM9

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

Summary for 1IM9

• Entry DOI: 10.2210/pdb1im9/pdb
• Related: 1NKR 1QQD
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, CW-4 CW*0401 ALPHA CHAIN, Beta-2 microglobulin, HLA-Cw4-specific peptide, ... (5 entities in total)
• Functional Keywords: protein-protein complex, immunoglobulin domain, antiparallel beta sheet, alpha helix, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P30504; Secreted: P61769; Cell membrane; Single-pass type I membrane protein: P43626
• Total number of polymer chains: 7
• Total formula weight: 115057.53

Authors

Fan, Q.R.,Long, E.O.,Wiley, D.C. (deposition date: 2001-05-10, release date: 2001-05-30, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)