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Development of solid state NMR methods for describing high resolution ligand binding site structure for a 7TMD GPCR
Reference
B11111
Principal Investigator / Supervisor
Professor Anthony Watts
Co-Investigators /
Co-Supervisors
Dr Philip Williamson
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
171,392
Status
Completed
Type
Research Grant
Start date
01/10/1999
End date
31/03/2003
Duration
42 months
Abstract
Over the last 6 years we have developed solid state NMR methods for resolving: structural details of membrane-embedded peptides; dynamic, structural and orientational details for ligands at their site of action in large (Mr>>30k) membrane-embedded fully functional receptors. In this new application, these two approaches will be combined to develop general methods for resolving ligand-receptor structural descriptions, using the human neurotensin (13-mer peptide) receptor (NTR), a member of the 7TMD, GPCR family, expressed in plasma membranes of E. coli with a His-tag to aid purification. Here, the potential for protein labelling (uniformly and specifically) exists, to combine with peptides containing similar NMR visible, stable isotopes.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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