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Integrating structural and mutagenesis data to elucidate GPCR ligand binding

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Integrating structural and mutagenesis data to elucidate GPCR ligand binding. / Munk, Christian; Harpsøe, Kasper; Hauser, Alexander S; Isberg, Vignir; Gloriam, David E.

In: Current Opinion in Pharmacology, Vol. 30, 10.2016, p. 51-58.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Munk, C, Harpsøe, K, Hauser, AS, Isberg, V & Gloriam, DE 2016, 'Integrating structural and mutagenesis data to elucidate GPCR ligand binding' Current Opinion in Pharmacology, vol. 30, pp. 51-58. https://doi.org/10.1016/j.coph.2016.07.003

APA

Munk, C., Harpsøe, K., Hauser, A. S., Isberg, V., & Gloriam, D. E. (2016). Integrating structural and mutagenesis data to elucidate GPCR ligand binding. Current Opinion in Pharmacology, 30, 51-58. https://doi.org/10.1016/j.coph.2016.07.003

Vancouver

Munk C, Harpsøe K, Hauser AS, Isberg V, Gloriam DE. Integrating structural and mutagenesis data to elucidate GPCR ligand binding. Current Opinion in Pharmacology. 2016 Oct;30:51-58. https://doi.org/10.1016/j.coph.2016.07.003

Author

Munk, Christian ; Harpsøe, Kasper ; Hauser, Alexander S ; Isberg, Vignir ; Gloriam, David E. / Integrating structural and mutagenesis data to elucidate GPCR ligand binding. In: Current Opinion in Pharmacology. 2016 ; Vol. 30. pp. 51-58.

Bibtex

@article{1a8f7d350c5547cdbbd3276a41ec1879,
title = "Integrating structural and mutagenesis data to elucidate GPCR ligand binding",
abstract = "G protein-coupled receptors (GPCRs) represent the largest family of human membrane proteins, as well as drug targets. A recent boom in GPCR structural biology has provided detailed images of receptor ligand binding sites and interactions on the molecular level. An ever-increasing number of ligands is reported that exhibit activity through multiple receptors, binding in allosteric sites, and bias towards different intracellular signalling pathways. Furthermore, a wealth of single point mutants has accumulated in literature and public databases. Integrating these structural and mutagenesis data will help elucidate new GPCR ligand binding sites, and ultimately design drugs with tailored pharmacological activity.",
author = "Christian Munk and Kasper Harps{\o}e and Hauser, {Alexander S} and Vignir Isberg and Gloriam, {David E}",
note = "Copyright {\circledC} 2016 Elsevier Ltd. All rights reserved.",
year = "2016",
month = "10",
doi = "10.1016/j.coph.2016.07.003",
language = "English",
volume = "30",
pages = "51--58",
journal = "Current Opinion in Pharmacology",
issn = "1471-4892",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Integrating structural and mutagenesis data to elucidate GPCR ligand binding

AU - Munk, Christian

AU - Harpsøe, Kasper

AU - Hauser, Alexander S

AU - Isberg, Vignir

AU - Gloriam, David E

N1 - Copyright © 2016 Elsevier Ltd. All rights reserved.

PY - 2016/10

Y1 - 2016/10

N2 - G protein-coupled receptors (GPCRs) represent the largest family of human membrane proteins, as well as drug targets. A recent boom in GPCR structural biology has provided detailed images of receptor ligand binding sites and interactions on the molecular level. An ever-increasing number of ligands is reported that exhibit activity through multiple receptors, binding in allosteric sites, and bias towards different intracellular signalling pathways. Furthermore, a wealth of single point mutants has accumulated in literature and public databases. Integrating these structural and mutagenesis data will help elucidate new GPCR ligand binding sites, and ultimately design drugs with tailored pharmacological activity.

AB - G protein-coupled receptors (GPCRs) represent the largest family of human membrane proteins, as well as drug targets. A recent boom in GPCR structural biology has provided detailed images of receptor ligand binding sites and interactions on the molecular level. An ever-increasing number of ligands is reported that exhibit activity through multiple receptors, binding in allosteric sites, and bias towards different intracellular signalling pathways. Furthermore, a wealth of single point mutants has accumulated in literature and public databases. Integrating these structural and mutagenesis data will help elucidate new GPCR ligand binding sites, and ultimately design drugs with tailored pharmacological activity.

U2 - 10.1016/j.coph.2016.07.003

DO - 10.1016/j.coph.2016.07.003

M3 - Journal article

VL - 30

SP - 51

EP - 58

JO - Current Opinion in Pharmacology

JF - Current Opinion in Pharmacology

SN - 1471-4892

ER -

ID: 165016790