Tethering chemistry and K+ channels
dc.contributor.author | Morin, Trevor J. | |
dc.contributor.author | Kobertz, William R. | |
dc.date | 2022-08-11T08:08:52.000 | |
dc.date.accessioned | 2022-08-23T16:10:35Z | |
dc.date.available | 2022-08-23T16:10:35Z | |
dc.date.issued | 2008-06-11 | |
dc.date.submitted | 2009-02-24 | |
dc.identifier.citation | J Biol Chem. 2008 Sep 12;283(37):25105-9. Epub 2008 Jun 9. <a href="http://dx.doi.org/10.1074/jbc.R800033200">Link to article on publisher's site</a> | |
dc.identifier.issn | 0021-9258 (Print) | |
dc.identifier.doi | 10.1074/jbc.R800033200 | |
dc.identifier.pmid | 18541528 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32966 | |
dc.description.abstract | Voltage-gated K+ channels are dynamic macromolecular machines that open and close in response to changes in membrane potential. These multisubunit membrane-embedded proteins are responsible for governing neuronal excitability, maintaining cardiac rhythmicity, and regulating epithelial electrolyte homeostasis. High resolution crystal structures have provided snapshots of K+ channels caught in different states with incriminating molecular detail. Nonetheless, the connection between these static images and the specific trajectories of K+ channel movements is still being resolved by biochemical experimentation. Electrophysiological recordings in the presence of chemical modifying reagents have been a staple in ion channel structure/function studies during both the pre- and post-crystal structure eras. Small molecule tethering agents (chemoselective electrophiles linked to ligands) have proven to be particularly useful tools for defining the architecture and motions of K+ channels. This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K+ channel protein complexes. | |
dc.language.iso | en_US | |
dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=18541528&dopt=Abstract">Link to Article in PubMed</a> | |
dc.relation.url | http://dx.doi.org/10.1074/jbc.R800033200 | |
dc.subject | Animals; Biochemistry; Crystallography, X-Ray; Cysteine; Electrophysiology; Humans; Ion Channel Gating; Ligands; Membrane Potentials; Models, Biological; Models, Chemical; Molecular Conformation; Neurons; Potassium Channels, Voltage-Gated; Protein Conformation | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Tethering chemistry and K+ channels | |
dc.type | Journal Article | |
dc.source.journaltitle | The Journal of biological chemistry | |
dc.source.volume | 283 | |
dc.source.issue | 37 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1517 | |
dc.identifier.contextkey | 738110 | |
html.description.abstract | <p>Voltage-gated K+ channels are dynamic macromolecular machines that open and close in response to changes in membrane potential. These multisubunit membrane-embedded proteins are responsible for governing neuronal excitability, maintaining cardiac rhythmicity, and regulating epithelial electrolyte homeostasis. High resolution crystal structures have provided snapshots of K+ channels caught in different states with incriminating molecular detail. Nonetheless, the connection between these static images and the specific trajectories of K+ channel movements is still being resolved by biochemical experimentation. Electrophysiological recordings in the presence of chemical modifying reagents have been a staple in ion channel structure/function studies during both the pre- and post-crystal structure eras. Small molecule tethering agents (chemoselective electrophiles linked to ligands) have proven to be particularly useful tools for defining the architecture and motions of K+ channels. This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K+ channel protein complexes.</p> | |
dc.identifier.submissionpath | gsbs_sp/1517 | |
dc.contributor.department | Department of Biochemistry and Molecular Pharmacology | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 25105-9 |