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Molecular recognition subunit interactions and structure-function analysis of recombinant human and plant PDCs

Reference	B15672
Principal Investigator / Supervisor	Professor John Lindsay
Co-Investigators / Co-Supervisors	Professor Richard Cogdell, Dr Adrian Lapthorn, Professor Nicholas Price, Professor Steve Yeaman
Institution	University of Glasgow
Department	IBLS Division of Biochemistry & Molecula
Funding type	Research
Value (£)	419,316
Status	Completed
Type	Research Grant
Start date	01/03/2002
End date	30/09/2005
Duration	43 months

Abstract

The major specific aims of this project are as follows: to utilise recombinant domains/didomains of human/plant E2s (and E3BPs) to obtain crystal structures for these domains and evaluate the stoichiometry, specificity and affinity of E1 and E3 binding; to solve the structure of full-length E3BP alone or as the E3/E3BP subcomplex; to use SPR and ITC to map critical regions of the inner E2 lipoyl domain required for recognition by its cognate complex-specific kinases; to utilise engineered forms of E2 to determine how domain organisation/spatial geometry affects kinase/phosphatase-E1 interactions and phosphorylation efficiency; to conduct a comparative structure-function analysis of the unique plant organelle and complex-specific forms of E2 and E3.

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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