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PEDS Advance Access originally published online on July 25, 2005
Protein Engineering Design and Selection 2005 18(8):359-364; doi:10.1093/protein/gzi048
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© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org

REVIEW

Engineering allosteric protein switches by domain insertion

Marc Ostermeier

Department of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA

E-mail: oster{at}jhu.edu

Domain insertion is proving to be an effective way to construct hybrid proteins exhibiting switch-like behavior. In this strategy, two existing domains, the first exhibiting a signal recognition function and the second containing the function to be modulated, are fused such that the recognition of the signal by the first domain is transmitted to the second domain, thereby modulating its activity. Recent directed evolution experiments indicate that the structural space comprised of the recombination of unrelated protein domains may be rich in switching behavior, particularly when the circular permutation of domains is also employed. This bodes well for potential basic science, sensing and therapeutic applications of molecular switches.

Keywords: allosteric protein switches/domain insertion/molecular switches

Received May 20, 2005; revised July 1, 2005; accepted July 4, 2005.

Edited by Dan Tawfik


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