1efx
From Proteopedia
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STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3
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Overview
Target cell lysis is regulated by natural killer (NK) cell receptors that, recognize class I MHC molecules. Here we report the crystal structure of, the human immunoglobulin-like NK cell receptor KIR2DL2 in complex with its, class I ligand HLA-Cw3 and peptide. KIR binds in a nearly orthogonal, orientation across the alpha1 and alpha2 helices of Cw3 and directly, contacts positions 7 and 8 of the peptide. No significant conformational, changes in KIR occur on complex formation. The receptor footprint on HLA, overlaps with but is distinct from that of the T-cell receptor. Charge, complementarity dominates the KIR/HLA interface and mutations that disrupt, interface salt bridges substantially diminish binding. Most contacts in, the complex are between KIR and conserved HLA-C residues, but a hydrogen, bond between Lys 44 of KIR2DL2 and Asn 80 of Cw3 confers the allotype, specificity. KIR contact requires position 8 of the peptide to be a, residue smaller than valine. A second KIR/HLA interface produced an, ordered receptor-ligand aggregation in the crystal which may resemble, receptor clustering during immune synapse formation.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1EFX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand., Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD, Nature. 2000 Jun 1;405(6786):537-43. PMID:10850706
Page seeded by OCA on Fri Feb 15 15:43:04 2008
