Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.495042
Title: Ligand interactions of glutamate receptor 2 studied by NMR
Author: Edwards, Rachel
Awarding Body: UNIVERSITY OF MANCHESTER
Current Institution: University of Manchester
Date of Award: 2008
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Abstract:
Neurotransmission is the action of communication between neurons; the most common neurotransmitter in the mammalian CNS is glutamate. Excessive activation of glutamate receptors have been implicated in a number of neurodegenerative diseases; they are therefore of great interest for investigation as drug targets. The ionotropic glutamate receptor GluR2 has previously been expressed as a soluble construct representing the ligand binding domain known as S1S2J. GluR2 S1S2J contains two separate binding sites for different types of ligands; the glutamate binding site and the allosteric modulator binding site which is located the dimer interface formed between two GluR2 S1S2J monomers. Binding of ligands to the different sites has been implicated in two different mechanisms for receptor inactivation; both sites are targets for lead drug design. The GluR2 S1S2J construct has been studied in complex with its agonists and antagonists by X-ray crystallography however some questions remain about the exact structure of the ligand within the site and the allosteric modulator binding site has yet to be studied extensively.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.495042  DOI: Not available
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