NDLI: Polymorphic sites away from the Bw4 epitope that affect interaction of Bw4+ HLA-B with KIR3DL1.

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Polymorphic sites away from the Bw4 epitope that affect interaction of Bw4+ HLA-B with KIR3DL1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sanjanwala, Bharati Norman, Paul J. Parham, Peter Draghi, Monia Guethlein, Lisbeth A.
Description	Country affiliation: United States Author Affiliation: Sanjanwala B ( Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.)
Abstract	KIR3DL1 is a polymorphic, inhibitory NK cell receptor specific for the Bw4 epitope carried by subsets of HLA-A and HLA-B allotypes. The Bw4 epitope of HLA-B5101 and HLA-B1513 is determined by the NIALR sequence motif at positions 77, 80, 81, 82, and 83 in the alpha(1) helix. Mutation of these positions to the residues present in the alternative and nonfunctional Bw6 motif showed that the functional activity of the Bw4 epitopes of B5101 and B1513 is retained after substitution at positions 77, 80, and 81, but lost after substitution of position 83. Mutation of leucine to arginine at position 82 led to loss of function for B5101 but not for B1513. Further mutagenesis, in which B1513 residues were replaced by their B5101 counterparts, showed that polymorphisms in all three extracellular domains contribute to this functional difference. Prominent were positions 67 in the alpha(1) domain, 116 in the alpha(2) domain, and 194 in the alpha(3) domain. Lesser contributions were made by additional positions in the alpha(2) domain. These positions are not part of the Bw4 epitope and include residues shaping the B and F pockets that determine the sequence and conformation of the peptides bound by HLA class I molecules. This analysis shows how polymorphism at sites throughout the HLA class I molecule can influence the interaction of the Bw4 epitope with KIR3DL1. This influence is likely mediated by changes in the peptides bound, which alter the conformation of the Bw4 epitope.
ISSN	00221767
e-ISSN	15506606
Journal	The Journal of Immunology
Issue Number	9
Volume Number	181
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2008-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hla-b Antigens Genetics Metabolism Polymorphism, Genetic Immunology Receptors, Kir3dl1 Amino Acid Motifs Clone Cells Cytotoxicity Tests, Immunologic Biosynthesis Killer Cells, Natural Mutagenesis, Site-directed Peptides Protein Binding Comparative Study Research Support, N.i.h., Extramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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Polymorphic Sites Away From the Bw4 Epitope that Affect Interaction of Bw4+ HLA-B with KIR3DL1

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Polymorphic sites away from the Bw4 epitope that affect interaction of Bw4+ HLA-B with KIR3DL1.

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Polymorphic Sites Away From the Bw4 Epitope that Affect Interaction of Bw4+ HLA-B with KIR3DL1

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Polymorphic sites away from the Bw4 epitope that affect interaction of Bw4+ HLA-B with KIR3DL1.