Skip Navigation


Bioinformatics Advance Access originally published online on September 8, 2005
Bioinformatics 2005 21(21):3959-3962; doi:10.1093/bioinformatics/bti659
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow All Versions of this Article:
21/21/3959    most recent
bti659v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (4)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Cymerman, I. A.
Right arrow Articles by Bujnicki, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cymerman, I. A.
Right arrow Articles by Bujnicki, J. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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

Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Sci.Home page
P. Schafer, I. A. Cymerman, J. M. Bujnicki, and G. Meiss
Human lysosomal DNase II{alpha} contains two requisite PLD-signature (HxK) motifs: Evidence for a pseudodimeric structure of the active enzyme species
Protein Sci., January 1, 2007; 16(1): 82 - 91.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.