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- Title
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K<sup>b</sup>.
- Authors
Dam, Julie; Rongjin Guan, Julie; Natarajan, Kannan; Dimasi, Nazzareno; Chlewicki, Lukasz K.; Kranz, David M.; Schuck, Peter; Margulies, David H.; Mariuzza, Roy A.
- Abstract
The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2Kb. The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.
- Publication
Nature Immunology, 2003, Vol 4, Issue 12, p1213
- ISSN
1529-2908
- Publication type
Academic Journal
- DOI
10.1038/ni1006