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| Immunity Sep (1998); 9(3):337-44 | |
| Kinetics of interaction of HLA-C ligands with natural killer cell inhibitory receptors. | |
| Vales-Gomez M, Reyburn HT, Mandelboim M, Strominger JL | |
| Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA. | |
| Abstract: The recognition of HLA-C molecules by specific inhibitory receptors is a crucial step in the regulation of natural killer (NK) cell function. Using soluble, recombinant HLA-C molecules and NK inhibitory receptors (NKIR, members of the immunoglobulin superfamily), we show that HLA-C binds to NKIR molecules with extremely fast association and dissociation rates, among the fastest of the immune system interactions so far studied. These kinetics may be essential for the biological function of NK cells, i.e., to facilitate the rapid immunosurveillance of cells for absent or diminished expression of class I MHC proteins. | |
| [PUBMED: 9768753] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |