1P4L

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

Summary for 1P4L

• Entry DOI: 10.2210/pdb1p4l/pdb
• Related: 1P1Z 1QO3 1VAC
• Descriptor: MHC CLASS I H-2KB HEAVY CHAIN, Beta-2-microglobulin, Ovalbumin peptide, ... (4 entities in total)
• Functional Keywords: natural killer receptor, mhc class i, c-type lectin-like domain, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887 P01012; Membrane; Single-pass type II membrane protein: Q64329
• Total number of polymer chains: 4
• Total formula weight: 58828.92

Authors

Dam, J.,Guan, R.,Natarajan, K.,Dimasi, N.,Mariuzza, R.A. (deposition date: 2003-04-23, release date: 2003-11-11, Last modification date: 2024-11-06)

Primary citation

Dam, J.,Guan, R.,Natarajan, K.,Dimasi, N.,Chlewicki, L.K.,Kranz, D.M.,Schuck, P.,Margulies, D.H.,Mariuzza, R.A.
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b).
Nat.Immunol., 4:1213-1222, 2003

PubMed 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-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.

PubMed: 14595439
DOI: 10.1038/ni1006

Experimental method

X-RAY DIFFRACTION (2.9 Å)