Award details

Nematode structural protein folding catalysts; structural characterisation and evaluation as targets for anti-helminthic development

Reference	C11671
Principal Investigator / Supervisor	Professor Malcolm Walkinshaw
Co-Investigators / Co-Supervisors	Professor Antony Page
Institution	University of Edinburgh
Department	Inst of Cell and Molecular Biology
Funding type	Research
Value (£)	129,961
Status	Completed
Type	Research Grant
Start date	01/11/1999
End date	31/10/2002
Duration	36 months

Abstract

The peptidyl prolyl isomerases (PPI) are a large family of ubiquitously expressed enzymes which control the rate-limiting step in protein folding. The cyclophilin class of PPIs are receptors for the immunosuppressant drug cyclosporin A (CsA) and have been extensively studied in the model nematode Caenorhabditis elegans revealing important cuticle collagen and muscle wall associated isoforms. CsA has anti-nematode effects directly related to cyclophilin inhibition. The aim of this project is to structurally characterise four enzymes involved in cuticle development in order to provide insight into the mechanism of protein folding, and to use the structural information of these and related enzymes to design and test inhibitory ligands which will specifically affect nematode development thus providing potentially new classes of anti- parasitic drugs. (Joint with grant C12229).

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
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

Associated awards:

C12229 Nematode structural protein folding catalysts; structural characterisation and evaluation as targets for anti-helminthic development

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