1qo3
From Proteopedia
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Gene: | H-2D (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:16:36 2008
