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BBSRC DTA Studentship : Crystallographic and functional studies of a Ca2+ triggered Ras GTPase activating protein

Reference	BBS/E/B/0000L968
Principal Investigator / Supervisor	Professor Len Stephens
Co-Investigators / Co-Supervisors
Institution	Babraham Institute
Department	Babraham Institute Department
Funding type	Research
Value (£)	37,341
Status	Completed
Type	Institute Project
Start date	01/10/2004
End date	30/09/2007
Duration	36 months

Abstract

Ras GTPase-activating proteins (Ras GAPs) negatively regulate Ras GTPases that are human proto-oncogenes. In up to 30% of human tumours Ras is mutated to an active form resistant to the action of GAPs, this active form of Ras is associated with the development and maintenance of tumours. There are a number of different types of Ras GAPs and the structure of the domain that catalyses the GTPase activity of Ras, the GAP-related domain (GRD), has been determined for p120 Ras GAP and the important tumour suppressor NF1. However, no structural information about the GAP1 family of Ras GAPs is known, and no full-length Ras GAP of any family has been crystallised. We wish to gain structural and biophysical knowledge of CAPRI, a Ca2+-triggered Ras GAP, in order to discover how this protein works and increase our knowledge of the Ras-Ras GAP interaction. As a result our understanding of how oncogenic Ras operates will also be increased.

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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