Linked Life Data

15046719

Source:http://linkedlifedata.com/resource/pubmed/id/15046719

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-3-29
pubmed:abstractText
Voltage-gated sodium channels are members of a large family with similar pore structures. The mechanism of opening and closing is unknown, but structural studies suggest gating via bending of the inner pore helix at a glycine hinge. Here we provide functional evidence for this gating model for the bacterial sodium channel NaChBac. Mutation of glycine 219 to proline, which would strongly favor bending of the alpha helix, greatly enhances activation by shifting its voltage dependence -51 mV and slowing deactivation by 2000-fold. The mutation also slows voltage-dependent inactivation by 1200-fold. The effects are specific because substitutions of proline at neighboring positions and substitutions of other amino acids at position 219 have much smaller functional effects. Our results fit a model in which concerted bending at glycine 219 in the S6 segments of NaChBac serves as a gating hinge. This gating motion may be conserved in most members of this large ion channel protein family.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
859-65
pubmed:dateRevised
2009-10-1
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A gating hinge in Na+ channels; a molecular switch for electrical signaling.
pubmed:affiliation
Department of Pharmacology, Box 357280, University of Washington, Seattle, WA 98105, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.