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dc.contributor.author Chéron, Jean Baptiste -
dc.contributor.author Golebiowski, Jérôme -
dc.contributor.author Antonczak, Serge -
dc.contributor.author Fiorucci, Sébastien -
dc.date.available 2017-06-29T08:09:42Z -
dc.date.created 2017-04-20 -
dc.date.issued 2017 -
dc.identifier.issn 0887-3585 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/2093 -
dc.description.abstract All sweet-tasting compounds are detected by a single G-protein coupled receptor (GPCR), the heterodimer T1R2-T1R3, for which no experimental structure is available. The sweet taste receptor is a class C GPCR, and the recently published crystallographic structures of metabotropic glutamate receptor (mGluR) 1 and 5 provide a significant step forward for understanding structure-function relationships within this family. In this article, we recapitulate more than 600 single point site-directed mutations and available structural data to obtain a critical alignment of the sweet taste receptor sequences with respect to other class C GPCRs. Using this alignment, a homology 3D-model of the human sweet taste receptor is built and analyzed to dissect out the role of key residues involved in ligand binding and those responsible for receptor activation. Proteins 2017; 85:332–341. © 2016 Wiley Periodicals, Inc. © 2016 Wiley Periodicals, Inc. -
dc.publisher John Wiley and Sons Inc. -
dc.title The anatomy of mammalian sweet taste receptors -
dc.type Article -
dc.identifier.doi 10.1002/prot.25228 -
dc.identifier.scopusid 2-s2.0-85010378578 -
dc.identifier.bibliographicCitation Proteins: Structure, Function and Bioinformatics, v.85, no.2, pp.332 - 341 -
dc.citation.endPage 341 -
dc.citation.number 2 -
dc.citation.startPage 332 -
dc.citation.title Proteins: Structure, Function and Bioinformatics -
dc.citation.volume 85 -
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Appears in Collections:
ETC 1. Journal Articles
Department of Brain Sciences ETC 1. Journal Articles

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