Award details

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

Reference	C12229
Principal Investigator / Supervisor	Professor Antony Page
Co-Investigators / Co-Supervisors	Professor Malcolm Walkinshaw
Institution	University of Glasgow
Department	Wellcome Ctre for Molecular Parasitology
Funding type	Research
Value (£)	131,202
Status	Completed
Type	Research Grant
Start date	01/11/1999
End date	01/11/2002
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 body-wall muscle 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 a potentially new classes of antiparasitic drugs. (Joint with grant C11671).

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:

C11671 Nematode structural protein folding catalysts; structural characterisation and evaluation as targets for anti-helminthic development

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