Computational redesign of endonuclease DNA binding and cleavage specificity

Justin Ashworth (), James J. Havranek, Carlos M. Duarte, Django Sussman, Raymond J. Monnat, Barry L. Stoddard and David Baker ()
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Justin Ashworth: Howard Hughes Medical Institute and Department of Biochemistry
James J. Havranek: Howard Hughes Medical Institute and Department of Biochemistry
Carlos M. Duarte: Howard Hughes Medical Institute and Department of Biochemistry
Django Sussman: Fred Hutchinson Cancer Research Center
Raymond J. Monnat: University of Washington
Barry L. Stoddard: Fred Hutchinson Cancer Research Center
David Baker: Howard Hughes Medical Institute and Department of Biochemistry

Nature, 2006, vol. 441, issue 7093, 656-659

Abstract: Design for living Altering the specificity of DNA-cleaving enzymes could be useful in many medical or biotechnological applications, but it is quite a challenge in terms of computational protein design. Ashwell et al. have used computational redesign to alter the target-site specificity of the I-MsoI homing endonuclease, while maintaining wild-type binding affinity. The redesigned enzyme binds and cleaves the new DNA recognition site about 10,000 times more effectively than the wild-type enzyme, with target discrimination comparable to the original endonuclease. These results suggest that computational protein design methods can be used to create novel and highly specific endonucleases for gene therapy and other applications.

Date: 2006
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DOI: 10.1038/nature04818

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