Linked Life Data

20655880

Source:http://linkedlifedata.com/resource/pubmed/id/20655880

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-8-30
pubmed:abstractText
Voltage-sensor domains (VSDs) in voltage-gated ion channels are thought to regulate the probability that a channel adopts an open conformation by moving vertically in the lipid bilayer. Here we characterized the movement of the VSDs of the prokaryotic voltage-gated sodium channel, NaChBac. Substitution of residue T110, which is located on the extracellular side of the fourth transmembrane helix of the VSD, by cysteine resulted in the formation of a disulfide bond between adjacent subunits in the channel. Our results suggest that T110 residues in VSDs of adjacent subunits can come into close proximity, implying that the VSDs can move laterally in the membrane and constitute a mechanism that regulates channel activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1090-2104
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
399
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
341-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Evidence for lateral mobility of voltage sensors in prokaryotic voltage-gated sodium channels.
pubmed:affiliation
Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't