期刊
EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES
卷 21, 期 4, 页码 397-405出版社
ELSEVIER
DOI: 10.1016/j.ejps.2003.11.010
关键词
BEET; FRET; G protein-coupled receptor; arrestin
Bioluminescence (BEET)- and fluorescence resonance energy transfer (FRET) techniques have become integral approaches in studies of protein-protein interactions in living cells. They rely on non-radiative transfer of energy between donor and acceptor species that can be appended to the proteins of interest. These techniques display exquisite dependence on distance and orientation between the energy transfer partners. This means they are well suited to measure both small conformational changes in response to ligand binding between partner proteins that remain within a complex or more extensive translocations of proteins between cellular compartments that occur in response to cellular challenge. Introduction of both energy donor and acceptor into a single polypeptide can also allow the detection of ligand-induced conformational switches in monomeric proteins in the millisecond time scale. Many of these approaches are amenable to high throughput screening and the drug discovery process. G protein-coupled receptors (GPCRs) represent a key drug target class. Specific applications of resonance energy transfer techniques to the identification of ligands for this class of protein are highlighted to illustrate general principles. (C) 2004 Elsevier B.V. All rights reserved.
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