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Molecular basis for amino acid sensing by family C G‐protein‐coupled receptors
Author(s) -
Wellendorph P,
BräunerOsborne H
Publication year - 2009
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.2008.00078.x
Subject(s) - rhodopsin like receptors , g protein coupled receptor , receptor , metabotropic receptor , class c gpcr , metabotropic glutamate receptor , biochemistry , 5 ht1 receptor , immune receptor , 5 ht5a receptor , biology , gabbr1 , gpr18 , g protein , chemistry , microbiology and biotechnology , agonist , protease activated receptor 2 , cannabinoid receptor
Family C of human G‐protein‐coupled receptors (GPCRs) is constituted by eight metabotropic glutamate receptors, two γ‐aminobutyric acid type B (GABA B1–2 ) subunits forming the heterodimeric GABA B receptor, the calcium‐sensing receptor, three taste1 receptors (T1R1–3), a promiscuous L‐α‐amino acid receptor G‐protein‐coupled receptor family C, group 6, subtype A (GPRC6A) and seven orphan receptors. Aside from the orphan receptors, the family C GPCRs are dimeric receptors characterized by a large extracellular Venus flytrap domain which bind the endogenous agonists. Except from the GABA B1–2 and T1R2–3 receptor, all receptors are either activated or positively modulated by amino acids. In this review, we outline mutational, biophysical and structural studies which have elucidated the interaction of the amino acids with the Venus flytrap domains, molecular mechanisms of receptor selectivity and the initial steps in receptor activation.