1qqd
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(New page: 200px<br /> <applet load="1qqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqd, resolution 2.70Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:49, 12 November 2007
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CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR
Contents |
Overview
The crystal structure of the human class I major histocompatibility, complex molecule, human histocompatibility leukocyte antigen (HLA)-Cw4, the ligand for a natural killer (NK) cell inhibitory receptor, has been, determined, complexed with a nonameric consensus peptide (QYDDAVYKL)., Relative to HLA-A2, the peptide binding groove is widened around the COOH, terminus of the alpha 1 helix, which contains residues that determine the, specificity of HLA-Cw4 for the inhibitory NK receptor, KIR2D. The, structure reveals an unusual pattern of internal hydrogen bonding among, peptide residues. The peptide is anchored in four specificity pockets in, the cleft and secured by extensive hydrogen bonds between the peptide main, chain and the cleft. The surface of HLA-Cw4 has electrostatic, complementarity to the surface of the NK cell inhibitory receptor KIR2D.
Disease
Known diseases associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700], Psoriasis, early onset, susceptibility to OMIM:[142840]
About this Structure
1QQD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor., Fan QR, Wiley DC, J Exp Med. 1999 Jul 5;190(1):113-23. PMID:10429675
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