Allosteric modulation of G-protein coupled receptors

Anders A. Jensen, Tracy A Spalding

    101 Citationer (Scopus)

    Abstract

    The superfamily of G-protein coupled receptors (GPCRs) has more than 1000 members and is the largest family of proteins in the body. GPCRs mediate signalling of stimuli as diverse as light, ions, small molecules, peptides and proteins and are the targets for many pharmaceuticals. Most GPCR ligands are believed to activate (agonists) or inhibit (competitive antagonists) receptor signalling by binding the receptor at the same site as the endogenous agonist, the orthosteric site. In contrast, allosteric ligands modulate receptor function by binding to different regions in the receptor, allosteric sites. In recent years, combinatorial chemistry and high throughput screening have helped identify several allosteric GPCR modulators with novel structures, several of which already have become valuable pharmacological tools and may be candidates for clinical testing in the near future. This mini review outlines the current status and perspectives of allosteric modulation of GPCR function with emphasis on the pharmacology of endogenous and synthesised modulators, their receptor interactions and the therapeutic prospects of allosteric ligands compared to orthosteric ligands.
    OriginalsprogEngelsk
    TidsskriftEuropean Journal of Pharmaceutical Sciences
    Vol/bind21
    Udgave nummer4
    Sider (fra-til)407-20
    Antal sider14
    ISSN0928-0987
    DOI
    StatusUdgivet - 2004

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