Ras protein, a guanosine triphosphatase (GTPase), is a molecular switch in signal transduction pathways that control cell growth and differentiation. In human cells, point mutations in crucial regions of Ras can cause uncontrolled cell growth, or tumors. We are trying to solve the structure of the complex between active Ras protein (Ras-GMPPNP) and the Ras interacting domain of RalGDS (RalGDS-RID), a GDP dissociation stimulator of Ral protein (Ras like protein). Our lab has solved the active Ras structure and the structure of RalGDS-RID with the MAD method. We would like to obtain a co-crystal data set, which will allow us to solve the structure of the complex by the Molecular Replacement method.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6119453
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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