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1qo3
From Proteopedia
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COMPLEX BETWEEN NK CELL RECEPTOR LY49A AND ITS MHC CLASS I LIGAND H-2DD
Overview
Natural killer (NK) cell function is regulated by NK receptors that, interact with MHC class I (MHC-I) molecules on target cells. The murine NK, receptor Ly49A inhibits NK cell activity by interacting with H-2D(d), through its C-type-lectin-like NK receptor domain. Here we report the, crystal structure of the complex between the Ly49A NK receptor domain and, unglycosylated H-2D(d). The Ly49A dimer interacts extensively with two, H-2D(d) molecules at distinct sites. At one interface, a single Ly49A, subunit contacts one side of the MHC-I peptide-binding platform, presenting an open cavity towards the conserved glycosylation site on the, H-2D(d) alpha2 domain. At a second, larger interface, the Ly49A dimer, binds in a region overlapping the CD8-binding site. The smaller interface, probably represents the interaction between Ly49A on the NK cell and MHC-I, on the target cell, whereas the larger one suggests an interaction between, Ly49A and MHC-I on the NK cell itself. Both Ly49A binding sites on MHC-I, are spatially distinct from that of the T-cell receptor.
About this Structure
1QO3 is a Protein complex structure of sequences from Human immunodeficiency virus and Mus musculus with EDO as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand., Tormo J, Natarajan K, Margulies DH, Mariuzza RA, Nature. 1999 Dec 9;402(6762):623-31. PMID:10604468
Page seeded by OCA on Thu Nov 8 14:24:47 2007
