Award details

Development of solid state NMR methods for describing high resolution ligand binding site structure for a 7TMD GPCR

ReferenceB11111
Principal Investigator / Supervisor Professor Anthony Watts
Co-Investigators /
Co-Supervisors
Dr Philip Williamson
Institution University of Oxford
DepartmentBiochemistry
Funding typeResearch
Value (£) 171,392
StatusCompleted
TypeResearch Grant
Start date 01/10/1999
End date 31/03/2003
Duration42 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
terms and conditions of use (opens in new window)
export PDF file