UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyGraduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
2008-06-11Keywords
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 ConformationLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
J Biol Chem. 2008 Sep 12;283(37):25105-9. Epub 2008 Jun 9. Link to article on publisher's siteDOI
10.1074/jbc.R800033200Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32966PubMed ID
18541528Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1074/jbc.R800033200