Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-27
pubmed:abstractText
We report a strong coupling between permeation and gating in a mutant NMDA channel (NR1 N598Q-NR2A). The channel opens to two states that differ by their conductance and, surprisingly, by their selectivity for two permeant monovalent cations, Na+ and Cs+. The two open states are linked to the closed state via a cyclic gating reaction that proceeds preferentially in one direction under biionic conditions, indicating that the gating mechanism is not at equilibrium. The direction and the magnitude of this gating asymmetry can be accounted for by assuming that ions bound to a site in the permeation pathway influence the gating of this mutant channel, and that in the closed state, the channel site is accessible to internal cations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-77
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9010214-Animals, pubmed-meshheading:9010214-Cesium, pubmed-meshheading:9010214-Cloning, Molecular, pubmed-meshheading:9010214-Electric Conductivity, pubmed-meshheading:9010214-Female, pubmed-meshheading:9010214-Glycine, pubmed-meshheading:9010214-Ion Channel Gating, pubmed-meshheading:9010214-Membrane Potentials, pubmed-meshheading:9010214-Models, Biological, pubmed-meshheading:9010214-Mutagenesis, Site-Directed, pubmed-meshheading:9010214-N-Methylaspartate, pubmed-meshheading:9010214-Oocytes, pubmed-meshheading:9010214-Patch-Clamp Techniques, pubmed-meshheading:9010214-Protein Conformation, pubmed-meshheading:9010214-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:9010214-Recombinant Proteins, pubmed-meshheading:9010214-Sodium, pubmed-meshheading:9010214-Xenopus laevis
pubmed:year
1997
pubmed:articleTitle
Coupling of permeation and gating in an NMDA-channel pore mutant.
pubmed:affiliation
Ecole Normale Supérieure, Laboratoire de Neurobiologie, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't