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Crystal structure of HLA-Cw4, the ligand for a natural killer (NK) cell receptor, complexed with a nonameric consensus peptide (QYDDAVYKL, shown in red). The structure of HLA-Cw4 reveals an unusual peptide conformation and a widened peptide binding groove. The peptide is anchored in four specificity pockets in the cleft. The surface of HLA-Cw4 exhibits charge complementarity to the surface of the NK cell inhibitory receptor KIR2D. See related article in this issue by Fan et al,. pp 113-123.
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