1p4l | pdb_00001p4l
Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb
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Overview
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-2K(b). 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.
About this Structure
1P4L is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439
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