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PDBsum entry 1qqd
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Immune system
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PDB id
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1qqd
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of human histocompatibility leukocyte antigen (hla)-Cw4, A ligand for the kir2d natural killer cell inhibitory receptor.
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Authors
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Q.R.Fan,
D.C.Wiley.
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Ref.
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J Exp Med, 1999,
190,
113-123.
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PubMed id
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Abstract
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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.
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