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Ligand Binding Transmits Conformational Changes across the Membrane‐Spanning Region to the Intracellular Side of the 5‐HT 3 Serotonin Receptor
Author(s) -
Ilegems Erwin,
Pick Horst,
Deluz Cédric,
Kellenberger Stephan,
Vogel Horst
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500191
Subject(s) - förster resonance energy transfer , intracellular , biophysics , 5 ht receptor , chemistry , receptor , ionotropic effect , extracellular , green fluorescent protein , g protein coupled receptor , conformational change , ligand (biochemistry) , agonist , serotonin , fluorescence , biochemistry , microbiology and biotechnology , biology , physics , nmda receptor , quantum mechanics , gene
Conformational changes of channel activation : Five enhanced green fluorescent protein (EGFP) molecules (green cylinders) were integrated into the intracellular part of the homopentameric ionotropic 5‐HT 3 receptor. This allowed the detection of extracellular binding of fluorescent ligands (•) to EGFP by FRET, and also enabled the quantification of agonist‐induced conformational changes in the intracellular region of the receptor by homo‐FRET between EGFPs. The approach opens novel ways for probing receptor activation and functional screening of therapeutic compounds.