1p4l: Difference between revisions

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[[Image:1p4l.gif|left|200px]]
{{Seed}}
[[Image:1p4l.png|left|200px]]


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{{STRUCTURE_1p4l|  PDB=1p4l  |  SCENE=  }}  
{{STRUCTURE_1p4l|  PDB=1p4l  |  SCENE=  }}  


'''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''
===Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb===




==Overview==
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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.
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{{ABSTRACT_PUBMED_14595439}}


==About this Structure==
==About this Structure==
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[[Category: Mhc class i]]
[[Category: Mhc class i]]
[[Category: Natural killer receptor]]
[[Category: Natural killer receptor]]
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