Molecular basis for amino acid sensing by family C G-protein-coupled receptors

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Standard

Molecular basis for amino acid sensing by family C G-protein-coupled receptors. / Wellendorph, Petrine; Bräuner-Osborne, Hans.

I: British Journal of Pharmacology, Bind 156, Nr. 6, 2009, s. 869-884.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Wellendorph, P & Bräuner-Osborne, H 2009, 'Molecular basis for amino acid sensing by family C G-protein-coupled receptors', British Journal of Pharmacology, bind 156, nr. 6, s. 869-884. https://doi.org/10.1111/j.1476-5381.2008.00078.x

APA

Wellendorph, P., & Bräuner-Osborne, H. (2009). Molecular basis for amino acid sensing by family C G-protein-coupled receptors. British Journal of Pharmacology, 156(6), 869-884. https://doi.org/10.1111/j.1476-5381.2008.00078.x

Vancouver

Wellendorph P, Bräuner-Osborne H. Molecular basis for amino acid sensing by family C G-protein-coupled receptors. British Journal of Pharmacology. 2009;156(6):869-884. https://doi.org/10.1111/j.1476-5381.2008.00078.x

Author

Wellendorph, Petrine ; Bräuner-Osborne, Hans. / Molecular basis for amino acid sensing by family C G-protein-coupled receptors. I: British Journal of Pharmacology. 2009 ; Bind 156, Nr. 6. s. 869-884.

Bibtex

@article{500ea9e030ac11de87b8000ea68e967b,
title = "Molecular basis for amino acid sensing by family C G-protein-coupled receptors",
abstract = "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.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Petrine Wellendorph and Hans Br{\"a}uner-Osborne",
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",
year = "2009",
doi = "10.1111/j.1476-5381.2008.00078.x",
language = "English",
volume = "156",
pages = "869--884",
journal = "British Journal of Pharmacology",
issn = "0007-1188",
publisher = "Wiley",
number = "6",

}

RIS

TY - JOUR

T1 - Molecular basis for amino acid sensing by family C G-protein-coupled receptors

AU - Wellendorph, Petrine

AU - Bräuner-Osborne, Hans

N1 - 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

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1111/j.1476-5381.2008.00078.x

DO - 10.1111/j.1476-5381.2008.00078.x

M3 - Journal article

C2 - 19298394

VL - 156

SP - 869

EP - 884

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 6

ER -

ID: 12002118