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    The function of the amino terminal domain in NMDA receptor modulation

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    Authors
    Huggins, David J.
    Grant, Guy H.
    Issue Date
    2005
    Subjects
    glutamate
    receptors
    glycine
    zinc
    desensitization
    
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    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
    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
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jmgm.2004.11.006
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

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