Allosteric control of an ionotropic glutamate receptor with an optical switch
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...
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Published in | Nature chemical biology Vol. 2; no. 1; pp. 47 - 52 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
Nature Publishing Group US
01.01.2006
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
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Abstract | 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 allosteric control using synthetic optical switches. Our strategy is exemplified by a ligand-gated ion channel of central importance in neuroscience, the ionotropic glutamate receptor (iGluR). Using structure-based design, we have modified its ubiquitous clamshell-type ligand-binding domain to develop a light-activated channel, which we call LiGluR. An agonist is covalently tethered to the protein through an azobenzene moiety, which functions as the optical switch. The agonist is reversibly presented to the binding site upon photoisomerization, initiating clamshell domain closure and concomitant channel gating. Photoswitching occurs on a millisecond timescale, with channel conductances that reflect the photostationary state of the azobenzene at a given wavelength. Our device has potential uses not only in biology but also in bioelectronics and nanotechnology. |
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AbstractList | 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 allosteric control using synthetic optical switches. Our strategy is exemplified by a ligand-gated ion channel of central importance in neuroscience, the ionotropic glutamate receptor (iGluR). Using structure-based design, we have modified its ubiquitous clamshell-type ligand-binding domain to develop a light-activated channel, which we call LiGluR. An agonist is covalently tethered to the protein through an azobenzene moiety, which functions as the optical switch. The agonist is reversibly presented to the binding site upon photoisomerization, initiating clamshell domain closure and concomitant channel gating. Photoswitching occurs on a millisecond timescale, with channel conductances that reflect the photostationary state of the azobenzene at a given wavelength. Our device has potential uses not only in biology but also in bioelectronics and nanotechnology. |
Author | Numano, Rika Kramer, Richard H Gorostiza, Pau Trauner, Dirk Volgraf, Matthew Isacoff, Ehud Y |
Author_xml | – sequence: 1 givenname: Ehud Y surname: Isacoff fullname: Isacoff, Ehud Y organization: Department of Molecular and Cell Biology, University of California Divisions of Material and Physical Bioscience, Lawrence Berkeley National Laboratory – sequence: 2 givenname: Dirk surname: Trauner fullname: Trauner, Dirk organization: Department of Chemistry, University of California Divisions of Material and Physical Bioscience, Lawrence Berkeley National Laboratory – sequence: 3 givenname: Matthew surname: Volgraf fullname: Volgraf, Matthew organization: Department of Chemistry, University of California – sequence: 4 givenname: Pau surname: Gorostiza fullname: Gorostiza, Pau organization: Department of Molecular and Cell Biology, University of California – sequence: 5 givenname: Rika surname: Numano fullname: Numano, Rika organization: Department of Molecular and Cell Biology, University of California Laboratory Animal Research Center, Institute of Medical Science, The University of Tokyo – sequence: 6 givenname: Richard H surname: Kramer fullname: Kramer, Richard H organization: Department of Molecular and Cell Biology, University of California Divisions of Material and Physical Bioscience, Lawrence Berkeley National Laboratory |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16408092$$D View this record in MEDLINE/PubMed |
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Snippet | 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... |
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SubjectTerms | 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 |
Title | Allosteric control of an ionotropic glutamate receptor with an optical switch |
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