title: The voltage-sensor structure in a voltage-gated channel.
abstract: A recent electron paramagnetic resonance study of KvAP, a prokaryotic voltage-gated channel, in its lipid native environment has revealed the location of the transmembrane segments, the connecting loops and the relative position of the voltage-sensing charges. The results confirm that the previously reported crystal structure does not represent a native conformation and give us structural constraints that will help in determining the molecular structure of the voltage sensor.
authors.affiliation: Department of Physiology, D. Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA. fbezanil@ucla.edu
authors.forename: Francisco
authors.initials: F
authors.lastname: Bezanilla
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry; D015640:Ion Channel Gating / Q000502:physiology*; D008958:Models, Molecular; D024642:Potassium Channels, Voltage-Gated / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D019843:Archaeal Proteins; D024642:Potassium Channels, Voltage-Gated