Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
Right arrow Comments: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when Comments are posted
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 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 (11)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Jonassen, I.
Right arrow Articles by Taylor, W. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jonassen, I.
Right arrow Articles by Taylor, W. R.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics Vol. 18 no. 2 2002
Pages 362-367
© 2002 Oxford University Press

Structure motif discovery and mining the PDB

Inge Jonassen 1,*, Ingvar Eidhammer 1, Darrell Conklin 2 and William R. Taylor 1,3

1 Department of Informatics, University of Bergen, HIB, N5020 Bergen, Norway
2 ZymoGenetics Inc., 1201 Eastlake Avenue East, Seattle, WA 98102, USA
3 Division of Mathematical Biology, National Institute of Medical Research, Mill Hill, London, UK

Received on March 2, 2001 ; revised on September 6, 2001 ; accepted on September 6, 2001

Motivation: Many of the most interesting functional and evolutionary relationships among proteins are so ancient that they cannot be reliably detected through sequence analysis and are apparent only through a comparison of the tertiary structures. The conserved features can often be described as structural motifs consisting of a few single residues or Secondary Structure (SS) elements. Confidence in such motifs is greatly boosted when they are found in more than a pair of proteins.

Results: We describe an algorithm for the automatic discovery of recurring patterns in protein structures. The patterns consist of individual residues having a defined order along the protein’s backbone that come close together in the structure and whose spatial conformations are similar. The residues in a pattern need not be close in the protein’s sequence. The work described in this paper builds on an earlier reported algorithm for motif discovery. This paper describes a significant improvement of the algorithm which makes it very efficient. The improved efficiency allows us to use it for doing unsupervised learning of patterns occurring in small subsets in a large set of structures, a non-redundant subset of the Protein Data Bank (PDB) database of all known protein structures.

Availability: The program is freely available to academia, requests can be sent to Inge.Jonassen{at}ii.uib.no.

Contact: Inge.Jonassen{at}ii.uib.no

* To whom correspondence should be addressed.


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
BioinformaticsHome page
K. L. Jensen, M. P. Styczynski, I. Rigoutsos, and G. N. Stephanopoulos
A generic motif discovery algorithm for sequential data
Bioinformatics, January 1, 2006; 22(1): 21 - 28.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
K. Wang and R. Samudrala
FSSA: a novel method for identifying functional signatures from structural alignments
Bioinformatics, July 1, 2005; 21(13): 2969 - 2977.
[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.