Integrating structural and mutagenesis data to elucidate GPCR ligand binding

Christian Munk; Kasper Harpsøe; Alexander S Hauser; Vignir Isberg; David E Gloriam

doi:10.1016/j.coph.2016.07.003

Integrating structural and mutagenesis data to elucidate GPCR ligand binding

Christian Munk, Kasper Harpsøe, Alexander S Hauser, Vignir Isberg, David E Gloriam

LUKKET: Institut for Lægemiddeldesign og Farmakologi

27 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Current Opinion in Pharmacology
Vol/bind	30
Sider (fra-til)	51-58
Antal sider	8
ISSN	1471-4892
DOI	https://doi.org/10.1016/j.coph.2016.07.003
Status	Udgivet - 1 okt. 2016

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10.1016/j.coph.2016.07.003

Citationsformater

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AU - Munk, Christian

AU - Harpsøe, Kasper

AU - Hauser, Alexander S

AU - Isberg, Vignir

AU - Gloriam, David E

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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.

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DO - 10.1016/j.coph.2016.07.003

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JO - Current Opinion in Pharmacology

JF - Current Opinion in Pharmacology

ER -

Integrating structural and mutagenesis data to elucidate GPCR ligand binding

Abstract

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