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Bioinformatics Advance Access originally published online on September 8, 2005
Bioinformatics 2005 21(21):3959-3962; doi:10.1093/bioinformatics/bti659
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© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions{at}oxfordjournals.org

DNase II is a member of the phospholipase D superfamily

Iwona A. Cymerman 1, Gregor Meiss 2 and Janusz M. Bujnicki 1,*

1Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology Trojdena 4, 02-109 Warsaw, Poland
2Institute of Biochemistry, Justus-Liebig-University Giessen 35392 Giessen, Germany

*To whom correspondence should be addressed.

Motivation: DNase II is an endodeoxyribonuclease involved in apoptosis and essential for the mammalian development. Despite the understanding of biochemical properties of this enzyme, its structure and relationships to other protein families remain unknown.

Results: Using protein fold-recognition we found that DNase II exhibits a catalytic domain common to the phospholipase D superfamily. Our model explains the available experimental data and provides the first structural platform for sequence–function analyses of this important nuclease.

Contact: iamb{at}genesilico.pl

Supplementary information: ftp://genesilico.pl/iamb/models/DNasell/

Received on February 25, 2005; revised on July 16, 2005; accepted on September 1, 2005

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