Unknown

Dataset Information

0

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.

SUBMITTER: Munk C 

PROVIDER: S-EPMC6910865 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Integrating structural and mutagenesis data to elucidate GPCR ligand binding.

Munk Christian C   Harpsøe Kasper K   Hauser Alexander S AS   Isberg Vignir V   Gloriam David E DE  

Current opinion in pharmacology 20160729


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 ha  ...[more]

Similar Datasets

| S-EPMC5557796 | biostudies-literature
| S-EPMC7007187 | biostudies-literature
| S-EPMC5831789 | biostudies-literature
| S-EPMC7236428 | biostudies-literature
| S-EPMC7733796 | biostudies-literature
| S-EPMC6137713 | biostudies-literature
| S-EPMC6681916 | biostudies-literature
| S-EPMC3455371 | biostudies-literature
| S-EPMC6514967 | biostudies-literature
| S-EPMC5679736 | biostudies-literature