DIMERBOW: exploring possible GPCR dimer interfaces

AbstractG protein-coupled receptors (GPCRs) can form homo-, heterodimers and larger order oligomers that exert different functions than monomers. The pharmacological potential of such complexes is hampered by the limited information available on the type of complex formed and its quaternary structure. Several GPCR structures in the Protein Data Bank display crystallographic interfaces potentially compatible with physiological interactions. Here we present DIMERBOW, a database and web application aimed to visually browse the complete repertoire of potential GPCR dimers present in solved structures. The tool is suited to help finding the best possible structural template to model GPCR homomers. DIMERBOW is available at http://lmc.uab.es/dimerbow/.

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DIMERBOW: exploring possible GPCR dimer interfaces

Bioinformatics ◽

10.1093/bioinformatics/btaa117 ◽

2020 ◽

Vol 36 (10) ◽

pp. 3271-3272 ◽

Cited By ~ 1

Author(s):

Adrián García-Recio ◽

Gemma Navarro ◽

Rafael Franco ◽

Mireia Olivella ◽

Ramon Guixà-González ◽

...

Keyword(s):

Web Application ◽

Quaternary Structure ◽

Data Bank ◽

G Protein Coupled Receptors ◽

Supplementary Information ◽

Limited Information ◽

Structural Template ◽

Gpcr Dimer ◽

Pharmacological Potential ◽

G Protein Coupled

Abstract Motivation G protein-coupled receptors (GPCRs) can form homo-, heterodimers and larger order oligomers that exert different functions than monomers. The pharmacological potential of such complexes is hampered by the limited information available on the type of complex formed and its quaternary structure. Several GPCR structures in the Protein Data Bank display crystallographic interfaces potentially compatible with physiological interactions. Results Here, we present DIMERBOW, a database and web application aimed to visually browse the complete repertoire of potential GPCR dimers present in solved structures. The tool is suited to help finding the best possible structural template to model GPCR homomers. Availability and implementation DIMERBOW is available at http://lmc.uab.es/dimerbow/. Supplementary information Supplementary data are available at Bioinformatics online.

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New thoughts on the role of the βγ subunit in G protein signal transduction

Biochemistry and Cell Biology ◽

10.1139/o00-075 ◽

2000 ◽

Vol 78 (5) ◽

pp. 537-550 ◽

Cited By ~ 1

Author(s):

Barbara Vanderbeld ◽

Gregory M Kelly

Keyword(s):

Signal Transduction ◽

G Protein ◽

G Proteins ◽

G Protein Coupled Receptors ◽

Limited Information ◽

Α Subunit ◽

Downstream Effectors ◽

Receptor Signal ◽

G Protein Coupled

Heterotrimeric G proteins are involved in numerous biological processes, where they mediate signal transduction from agonist-bound G-protein-coupled receptors to a variety of intracellular effector molecules and ion channels. G proteins consist of two signaling moieties: a GTP-bound α subunit and a βγ heterodimer. The βγ dimer, recently credited as a significant modulator of G-protein-mediated cellular responses, is postulated to be a major determinant of signaling fidelity between G-protein-coupled receptors and downstream effectors. In this review we have focused on the role of βγ signaling and have included examples to demonstrate the heterogeneity in the heterodimer composition and its implications in signaling fidelity. We also present an overview of some of the effectors regulated by βγ and draw attention to the fact that, although G proteins and their associated receptors play an instrumental role in development, there is rather limited information on βγ signaling in embryogenesis.Key words: G protein, βγ subunit, G-protein-coupled receptor, signal transduction, adenylyl cyclase.

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