1im9
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(New page: 200px<br /> <applet load="1im9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1im9, resolution 2.80Å" /> '''Crystal structure o...)
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Revision as of 15:25, 12 November 2007
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Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1 bound to its MHC ligand HLA-Cw4
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700], Psoriasis, early onset, susceptibility to OMIM:[142840]
About this Structure
1IM9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex., Fan QR, Long EO, Wiley DC, Nat Immunol. 2001 May;2(5):452-60. PMID:11323700
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