2.50
Hdl Handle:
http://hdl.handle.net/10547/294525
Title:
The function of the amino terminal domain in NMDA receptor modulation
Authors:
Huggins, David J.; Grant, Guy H.
Abstract:
The authors have modelled dimers of the amino terminal domains of these receptors based on their homology with the extracellular dimer of a metabotropic glutamate receptor. Conserved cysteine residues, which have been highlighted as important in previous work, are shown to form a disulphide bridge, stabilizing a four-helix bundle between subunits. This establishes a hinge in the receptor. The model also highlights a zinc binding site in the binding crevice of the NR2a subunit of the receptor that stabilizes the open state of the amino terminal domain. The similar effect of ifenprodil is thus explained by its stabilization of the open state of the amino terminal domain (ATD). The presence of three histidine residues in the zinc site is used to explain the pH dependence of zinc inhibition.
Citation:
Huggins, D.J. and Grant, G.H. (2005) 'The function of the amino terminal domain in NMDA receptor modulation', Journal of Molecular Graphics and Modelling, 23(4), pp.381-388
Publisher:
Elsevier
Journal:
Journal of Molecular Graphics and Modelling
Issue Date:
2005
URI:
http://hdl.handle.net/10547/294525
DOI:
10.1016/j.jmgm.2004.11.006
Additional Links:
http://linkinghub.elsevier.com/retrieve/pii/S1093326304001093
Type:
Article
Language:
en
ISSN:
1093-3263
Appears in Collections:
Cell and Cryobiology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorHuggins, David J.en_GB
dc.contributor.authorGrant, Guy H.en_GB
dc.date.accessioned2013-06-25T14:53:44Z-
dc.date.available2013-06-25T14:53:44Z-
dc.date.issued2005-
dc.identifier.citationHuggins, D.J. and Grant, G.H. (2005) 'The function of the amino terminal domain in NMDA receptor modulation', Journal of Molecular Graphics and Modelling, 23(4), pp.381-388en_GB
dc.identifier.issn1093-3263-
dc.identifier.doi10.1016/j.jmgm.2004.11.006-
dc.identifier.urihttp://hdl.handle.net/10547/294525-
dc.description.abstractThe authors have modelled dimers of the amino terminal domains of these receptors based on their homology with the extracellular dimer of a metabotropic glutamate receptor. Conserved cysteine residues, which have been highlighted as important in previous work, are shown to form a disulphide bridge, stabilizing a four-helix bundle between subunits. This establishes a hinge in the receptor. The model also highlights a zinc binding site in the binding crevice of the NR2a subunit of the receptor that stabilizes the open state of the amino terminal domain. The similar effect of ifenprodil is thus explained by its stabilization of the open state of the amino terminal domain (ATD). The presence of three histidine residues in the zinc site is used to explain the pH dependence of zinc inhibition.en_GB
dc.language.isoenen
dc.publisherElsevieren_GB
dc.relation.urlhttp://linkinghub.elsevier.com/retrieve/pii/S1093326304001093en_GB
dc.rightsArchived with thanks to Journal of Molecular Graphics and Modellingen_GB
dc.subjectglutamateen_GB
dc.subjectreceptorsen_GB
dc.subjectglycineen_GB
dc.subjectzincen_GB
dc.subjectdesensitizationen_GB
dc.titleThe function of the amino terminal domain in NMDA receptor modulationen
dc.typeArticleen
dc.identifier.journalJournal of Molecular Graphics and Modellingen_GB
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