1zs8
From Proteopedia
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Crystal Structure of the Murine MHC Class Ib Molecule M10.5
Contents |
Overview
Neurons in the murine vomeronasal organ (VNO) express a family of class Ib, major histocompatibility complex (MHC) proteins (M10s) that interact with, the V2R class of VNO receptors. This interaction may play a direct role in, the detection of pheromonal cues that initiate reproductive and, territorial behaviors. The crystal structure of M10.5, an M10 family, member, is similar to that of classical MHC molecules. However, the M10.5, counterpart of the MHC peptide-binding groove is open and unoccupied, revealing the first structure of an empty class I MHC molecule. Similar to, empty MHC molecules, but unlike peptide-filled MHC proteins and, non-peptide-binding MHC homologs, M10.5 is thermally unstable, suggesting, that its groove is normally occupied. However, M10.5 does not bind, endogenous peptides when expressed in mammalian cells or when offered a, mixture of class I-binding peptides. The F pocket side of the M10.5 groove, is open, suggesting that ligands larger than 8-10-mer class I-binding, peptides could fit by extending out of the groove. Moreover, variable, residues point up from the groove helices, rather than toward the groove, as in classical MHC structures. These data suggest that M10s are unlikely, to provide specific recognition of class I MHC-binding peptides, but are, consistent with binding to other ligands, including proteins such as the, V2Rs.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1ZS8 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a pheromone receptor-associated MHC molecule with an open and empty groove., Olson R, Huey-Tubman KE, Dulac C, Bjorkman PJ, PLoS Biol. 2005 Aug;3(8):e257. Epub 2005 Jul 12. PMID:16089503
Page seeded by OCA on Mon Nov 12 20:40:08 2007
