Allosteric control of an ionotropic glutamate receptor with an optical switch

• Published in: Nature chemical biology Vol. 2; no. 1; pp. 47 - 52
• Main Authors: Isacoff, Ehud Y, Trauner, Dirk, Volgraf, Matthew, Gorostiza, Pau, Numano, Rika, Kramer, Richard H
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.01.2006; Nature Publishing Group
• Subjects: Allosteric Regulation; Animals; Azo Compounds - chemistry; Binding Sites; Biochemical Engineering; Biochemistry; Biology; Bioorganic Chemistry; Cell Biology; Cells, Cultured; Chemistry; Chemistry/Food Science; Crystallography, X-Ray; Cysteine - genetics; Cysteine - metabolism; Dose-Response Relationship, Radiation; Electrophysiology; Humans; Ion Channel Gating; Isomerism; Ligands; Light; Models, Chemical; Nanotechnology; Neurosciences - methods; Potassium; Proteins; Receptors, Glutamate - chemistry; Receptors, Glutamate - metabolism; Receptors, Glutamate - radiation effects; Ubiquitins - chemistry; United States > US; California

The precise regulation of protein activity is fundamental to life. The allosteric control of an active site by a remote regulatory binding site is a mechanism of regulation found across protein classes, from enzymes to motors to signaling proteins. We describe a general approach for manipulating all...