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Structure and dynamics of full length prion proteins anchored in lipid membranes
Reference
BS516471
Principal Investigator / Supervisor
Dr Teresa Pinheiro
Co-Investigators /
Co-Supervisors
Institution
University of Warwick
Department
Biological Sciences
Funding type
Research
Value (£)
257,756
Status
Completed
Type
Research Grant
Start date
14/05/2002
End date
13/07/2005
Duration
38 months
Abstract
The conversion of the cellular benign form of the prion protein (PrP) into a pathogenic isoform appears to be a key event in prion diseases. Despite solution structures of a few mammalian PrP and several studies addressing PrP conversion in solution, the molecular mechanism of this undesirable event is not understood. PrP is a GPI-anchored plasma membrane protein and it is recognised that the conversion of PrP is likely to occur at the plasma membrane or in the endosomal/lysosomal pathway. However, structural biophysical studies of PrP in lipid membranes are scarce. A strategy is proposed to study the structural properties of PrP in membranes and to identify membrane-associated conformations of PrP that might mediate PrP conversion.
Summary
unavailable
Committee
Closed Committee - Agri-food (AF)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Biology of Spongiform Encephalopathies - Phase 5 (BS5) [2001]
Funding Scheme
X – not Funded via a specific Funding Scheme
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