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- W3205476627 abstract "Bitter taste receptors (TAS2Rs) are a poorly understood subgroup of G protein-coupled receptors (GPCRs). The experimental structure of these receptors has yet to be determined, and key-residues controlling their function remain mostly unknown. We designed an integrative approach to improve comparative modeling of TAS2Rs. Using current knowledge on class A GPCRs and existing experimental data in the literature as constraints, we pinpointed conserved motifs to entirely re-align the amino-acid sequences of TAS2Rs. We constructed accurate homology models of human TAS2Rs. As a test case, we examined the accuracy of the TAS2R16 model with site-directed mutagenesis and in vitro functional assays. This combination of in silico and in vitro results clarifies sequence-function relationships and proposes functional molecular switches that encode agonist sensing and downstream signaling mechanisms within mammalian TAS2Rs sequences." @default.
- W3205476627 created "2021-10-25" @default.
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- W3205476627 date "2021-10-23" @default.
- W3205476627 modified "2023-10-13" @default.
- W3205476627 title "Functional molecular switches of mammalian G protein-coupled bitter-taste receptors" @default.
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- W3205476627 doi "https://doi.org/10.1007/s00018-021-03968-7" @default.
- W3205476627 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34687318" @default.
- W3205476627 hasPublicationYear "2021" @default.
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