Linked Life Data

8608005

Source:http://linkedlifedata.com/resource/pubmed/id/8608005

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-5-28
pubmed:abstractText
Single channel currents from recombinant N-methyl-D-aspartate (NMDA) receptors having an N-to-Q mutation in M2 reveal a divalent cation binding site that is near the entrance of the pore (approximately 0.2 through the electric field). Ca2+ rapidly binds to this site and readily permeates the channel, while Mg2+ binds more slowly and does not permeate as readily. In wild-type receptors, Mg2+ also blocks the current by occupying a site that is approximately 0.6 through the field. When the more external site is occupied by Ca2+, the conductance of the pore to NA+ is reduced but not abolished, perhaps by an electrostatic blocking mechanism. The site serves to enrich the fraction of NMDA receptor current carried by CA2+.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
869-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Identification of a high affinity divalent cation binding site near the entrance of the NMDA receptor channel.
pubmed:affiliation
Department of Biophysical Sciences, State University of New York at Buffalo 14214, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.