This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Glutamate receptor ion channels (GluRs), which convert a chemical signal into an electrical impulse, are essential components of central nervous system synapses. Binding of the chemical messenger, glutamate, to the extracellular ligand-binding domain (GluR S1S2) induces a conformational transition in the GluRs thereby opening the channel to allow ionic current to stimulate the nerve. Through agonist or antagonist binding the GluR S1S2 plays a key role in channel activation and desensitization. While crystal structures of the apo-state give a static picture of an open ligand-binding cleft, preliminary computational studies have suggested a larger degree of variation in the apo-structure. Initial pulsed ESR experiments are aimed at providing information on the distribution of lobe separation distances in apo and ligand bound states

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR016292-06
Application #
7420518
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2006-09-15
Project End
2007-08-31
Budget Start
2006-09-15
Budget End
2007-08-31
Support Year
6
Fiscal Year
2006
Total Cost
$4,596
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Jain, Rinku; Vanamee, Eva S; Dzikovski, Boris G et al. (2014) An iron-sulfur cluster in the polymerase domain of yeast DNA polymerase ?. J Mol Biol 426:301-8
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