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Mechanism of allosteric regulation and inhibition of Ser-Thr protein phosphatase 1
Reference
B14780
Principal Investigator / Supervisor
Professor Rudolf Allemann
Co-Investigators /
Co-Supervisors
Dr Jonathan Sanvoisin
Institution
University of Birmingham
Department
School of Chemistry
Funding type
Research
Value (£)
142,968
Status
Completed
Type
Research Grant
Start date
01/12/2000
End date
31/01/2003
Duration
26 months
Abstract
This project proposes to understand the mechanism by which a) PP1 cat is activated through allosteric site occupation, and b) how substrate specificity is modulated. c) To identify hydrolytically stable phosphopeptide substrate analogues to support structural studies of the substrate binding site d) To prepare tight-binding ligands for the allosteric site that modulate the substrate activity of the phosphopeptides and the inhibitory activity of the phosphopeptide analogues in a parallel manner. e) To begin to investigate the activation of the PPI cat-Inhibitor-1 complex by PP2A.
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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