1P1Z
X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO ITS MHC CLASS I LIGAND H-2Kb
Summary for 1P1Z
Entry DOI | 10.2210/pdb1p1z/pdb |
Related | 1JA3 1QO3 |
Descriptor | H-2 class I histocompatibility antigen, K-B alpha chain, Beta-2-microglobulin, Ovalbumin peptide, ... (4 entities in total) |
Functional Keywords | nk, kb, mhc, antigenic peptide, ly49, ova, 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 | 58686.60 |
Authors | Dimasi, N.,Natarajan, K.,Rangjin, G.,Dam, J.,Margulies, D.H.,Mariuzza, R.A. (deposition date: 2003-04-14, release date: 2003-11-11, Last modification date: 2024-10-16) |
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 Cited by 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: 14595439DOI: 10.1038/ni1006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.26 Å) |
Structure validation
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