Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1–HLA-Cw4 complex View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-05

AUTHORS

Qing R. Fan, Eric O. Long, Don C. Wiley

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. More... »

PAGES

452

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/87766

DOI

http://dx.doi.org/10.1038/87766

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1008531433

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11323700


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