Molecular basis for amino acid sensing by family C G-protein-coupled receptors
Research output: Contribution to journal › Journal article › Research › peer-review
Family C of human G-protein-coupled receptors (GPCRs) is constituted by eight metabotropic glutamate receptors, two gamma-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-alpha;-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.
Original language | English |
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Journal | British Journal of Pharmacology |
Volume | 156 |
Issue number | 6 |
Pages (from-to) | 869-884 |
ISSN | 0007-1188 |
DOIs | |
Publication status | Published - 2009 |
Bibliographical note
Keywords: G-protein-coupled receptors; family C; metabotropic glutamate receptors; calcium-sensing receptor; GABA(B) receptor; T1R1 taste receptor; GPRC6A receptor; amino acid sensing; mutations
- Former Faculty of Pharmaceutical Sciences
Research areas
ID: 12002118