Structural and functional characterization of the small GTPase Rheb and its complex with the GTPase activating protein TSC2-GAP.
Published: 2007
Language: eng
Number of pages: 92
ISBN-13: 9780494274859
Description: Rheb proteins represent a novel and unique family of the Ras GTPase superfamily in both their primary and tertiary structural features. Unlike other GAPs (GTPase Activating Proteins), TSC2-GAP does not have the "arginine finger", which was thought to be crucial for GAP catalysis. In order to elucidate the potentially unique GTP hydrolysis mechanism employed by the Rheb-TSC2-GAP system, Rheb and TSC2-GAP are purified from E. coli and subjected to biochemical and structural characterization. Fluorescent kinetic analysis of Rheb reveals a high nucleotide binding affinity. Far-UV circular dichroism spectroscopy indicates that the folded TSC2-GAP constructs are alpha-helical proteins. Crystals of one TSC2-GAP construct diffracted to 8 A at room temperature. Although one of the purified TSC2-GAP constructs co-eluted with purified Rheb on a size exclusion column, the interaction seems to be non-specific.
Notes: Source: Masters Abstracts International, Volume: 45-06, page: 3077.

Thesis (M.Sc.)--University of Toronto, 2007.

Electronic version licensed for access by U. of T. users.

ROBARTS MICROTEXT copy on microfiche.