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Structural analysis of the phosphoinositide- and inositol 1345-tetrakisphosphate-binding Ras/Rap GAP GAP1IP4BP

Reference	C13862
Principal Investigator / Supervisor	Professor Peter Cullen
Co-Investigators / Co-Supervisors	Professor R Brady, Dr Gyles Cozier
Institution	University of Bristol
Department	Biochemistry
Funding type	Research
Value (£)	179,204
Status	Completed
Type	Research Grant
Start date	01/09/2000
End date	01/09/2003
Duration	36 months

Abstract

GAP1IP4BP is a plasma membrane localised Ras and Rap GTPase-activating protein. Structurally it is composed of N-terminal C2 domains, a catalytic Ras GAP- related domain (GRD) and a C-terminal pleckstrin homology (PH) domain that forms a binding site for inositol 1,3,4,5 tetrakisphosphate (IP4) and the phosphoinositides (PI's) phosphatidylinositol 4,5-bisphospate and phosphatidylinositol 3,4,5-trisphosphate. The aims of this proposal are: 1) to characterise the basis GAP activity of GAP1IP4BP and address the mechanism which allows it to stimulate the GTPase activity of Ras and Rap; 2) extend our examination of the molecular interactions that are required for the plasma membrane association of GAP1IP4BP; and 3) obtain structural information by X-ray crystallography, of the GAP1IP4BP GRD and PH domain.

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

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