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dc.contributor.authorOlson, Rich
dc.contributor.authorHuey-Tubman, Kathryn E
dc.contributor.authorDulac, Catherine
dc.contributor.authorBjorkman, Pamela J.
dc.date.accessioned2010-10-04T19:24:24Z
dc.date.issued2005
dc.identifier.citationOlson, Rich, Kathryn E. Huey-Tubman, Catherine Dulac, and Pamela J. Bjorkman. 2005. Structure of a pheromone receptor-associated MHC molecule with an open and empty groove. PLoS Biology 3(8): e257.en_US
dc.identifier.issn1544-9173en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:4456979
dc.description.abstractNeurons 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.en_US
dc.description.sponsorshipMolecular and Cellular Biologyen_US
dc.language.isoen_USen_US
dc.publisherPublic Library of Scienceen_US
dc.relation.isversionofdoi:10.1371/journal.pbio.0030257en_US
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1174912/pdf/en_US
dash.licenseLAA
dc.subjectbiophysicsen_US
dc.subjectimmunologyen_US
dc.subjectneuroscienceen_US
dc.subjectbiochemistryen_US
dc.subjectin vitroen_US
dc.subjectmolecular biologyen_US
dc.subjectstructural biologyen_US
dc.titleStructure of a Pheromone Receptor-Associated MHC Molecule with an Open and Empty Grooveen_US
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden_US
dc.relation.journalPLoS Biologyen_US
dash.depositing.authorDulac, Catherine
dc.date.available2010-10-04T19:24:24Z
dc.identifier.doi10.1371/journal.pbio.0030257*


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