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Bioinformatics Advance Access originally published online on December 16, 2004
Bioinformatics 2005 21(8):1308-1310; doi:10.1093/bioinformatics/bti227
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© The Author 2004. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions{at}oupjournals.org

Structural drift: a possible path to protein fold change

S. Sri Krishna 2 and Nick V. Grishin 1,2,*

1Howard Hughes Medical Institute, University of Texas Southwestern Medical Center 5323, Harry Hines Blvd, Dallas, TX 75390-9050, USA
2Department of Biochemistry, University of Texas Southwestern Medical Center 5323, Harry Hines Blvd, Dallas, TX 75390-9050, USA

*To whom correspondence should be addressed.

Summary: Along with their mutating sequences, protein structures change in time. Analyzing a formate dehydrogenase domain that is evolutionarily related to ferredoxin, but simultaneously contains all the structural elements of a ß-Grasp fold, we illustrate here a mechanism termed as structural drift, by which changes to a protein fold can occur.

Contact: grishin{at}chop.swmed.edu


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