PULSED ESR STUDY OF CONFORMATIONAL CHANGES OF A GLUTAMATE BINDING DOMAIN

这个子项目是众多研究子项目之一

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.