Model Building Predicts An Additional Conformational Switch When GTP Binds To The Cdc42Hs Protein

Michael J. Sutcliffe*, Joanna Feltham¤, Richard A. Cerione¤, and Robert E. Oswald¤

*Department of Chemistry
University of Leicester
Leicester, LE1 7RH, UK
¤Department of Pharmacology
College of Veterinary Medicine
Cornell University
Ithaca, NY 14853 USA

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Abstract
The human Cdc42Hs protein is homologous to but contains a thirteen residue insertion with respect to the ras subfamily of GTP-binding proteins. The possible role of this region of structure has been investigated by model building. These studies suggest that this region could act as a conformational switch - in the "on" conformation, it both covers the nucleotide binding site and forms an extension to the likely effector binding site; in the "off" conformation it is no longer able to bind effector.

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This paper has published as:

M.J. Sutcliffe, J. Feltham, R.A. Cerione, & R.E. Oswald (1995) Model building predicts an additional conformational switch when GTP binds to the Cdc42Hs protein. Prot. Peptide Lett., 1, 84-91.

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Title Page
Introduction
Methods
Results and Discussion
Summary
References
Acknowledgements