Linked Life Data

15464024

Source:http://linkedlifedata.com/resource/pubmed/id/15464024

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2004-10-6
pubmed:abstractText
N-Methyl-D-aspartate (NMDA) receptor function is modulated by a wide variety of compounds, several of which appear to bind to globular extracellular amino terminal subunit domains (ATDs). This review focuses on modulators with putative binding sites in ATDs of NMDA receptor subunits, and potential mechanisms by which these compounds exert their effects on receptor function. With an overview that stresses several themes, we explore evidence that the ATDs of NR2 subunits appear to bind modulatory compounds in the cleft of a clamshell-like structure that is analogous to the ligand-binding domain. This modulation influences NMDA receptor function only partially, is dependent on extracellular pH, and affects receptor desensitization. Modulation of the NMDA receptor by the ATD is considered within a framework of functional modularity of multisubunit ion channels. We also consider the potential importance of the ATD in assembly of the receptor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
500
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-11
pubmed:dateRevised
2011-9-22
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Amino terminal domain regulation of NMDA receptor function.
pubmed:affiliation
Department of Neurobiology, University of Pittsburgh School of Medicine, E1456 BST, Pittsburgh, PA 15261, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural