Integrating structural and mutagenesis data to elucidate GPCR ligand binding

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

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

I: Current Opinion in Pharmacology, Bind 30, 10.2016, s. 51-58.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

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, bind 30, s. 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 okt.;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. I: Current Opinion in Pharmacology. 2016 ; Bind 30. s. 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}",

year = "2016",

month = oct,

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

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

C2 - 27475047

VL - 30

SP - 51

EP - 58

JO - Current Opinion in Pharmacology

JF - Current Opinion in Pharmacology

SN - 1471-4892

ER -

ID: 165016790