G protein-coupled receptor dimers: Functional consequences, disease states and drug targets
| Autor: | Matthew B. Dalrymple, Karin A. Eidne, Kevin D. G. Pfleger |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Pharmacology
Drug media_common.quotation_subject Allosteric regulation Computational biology Disease Biology Receptors G-Protein-Coupled Drug Delivery Systems Signalling Molecular level Allosteric Regulation Drug Design Animals Humans Pharmacology (medical) Receptor Dimerization Function (biology) media_common G protein-coupled receptor |
| Zdroj: | Pharmacology & Therapeutics. 118:359-371 |
| ISSN: | 0163-7258 |
| DOI: | 10.1016/j.pharmthera.2008.03.004 |
| Popis: | With an ever-expanding need for reliable therapeutic agents that are highly effective and exhibit minimal deleterious side effects, a greater understanding of the mechanisms underlying G protein-coupled receptor (GPCR) regulation is fundamental. GPCRs comprise more than 30% of all therapeutic drug targets and it is likely that this will only increase as more orphan GPCRs are identified. The past decade has seen a dramatic shift in the prevailing concept of how GPCRs function, in particular the growing acceptance that GPCRs are capable of interacting with one another at a molecular level to form complexes, with significantly different pharmacological properties to their monomeric selves. While the ability of like-receptors to associate and form homodimers raises some interesting mechanistic issues, the possibility that unlike-receptors could heterodimerise in certain tissue types, producing a functionally unique signalling complex that binds specific ligands, provides an invaluable opportunity to refine and redefine pharmacological interventions with greater specificity and efficacy. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect