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Control by phosphorylation: structural studies on phosphorylase kinase
Reference
B11748
Principal Investigator / Supervisor
Professor Dame Louise Johnson
Co-Investigators /
Co-Supervisors
Professor Martin Noble
Institution
University of Oxford
Department
Biochemistry
Funding type
Research
Value (£)
140,824
Status
Completed
Type
Research Grant
Start date
01/08/1999
End date
01/08/2002
Duration
36 months
Abstract
The structure determination of phosphorylase kinase kinase domain (PhK) in complex with peptide substrate and inactive ATP analogue has provided insights recognition, control and catalysis. New studies are aimed at providing a deeper analysis of the catalytic mechanism through site directed mutagenesis and structure determination of ternary complexes with transition state analogues and the complex with the protein substrate, glycogen phosphorylase. Structural studies on the full-length catalytic subunit in complex with calmodulin will elucidate the control of PhK by calcium. The structure of the quaternary holoenzyme complex (MW 1.3 MDa) will be investigated with combined X-ray and EM methods.
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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