Skip Navigation



Bioinformatics Advance Access published online on August 20, 2007
Bioinformatics, doi:10.1093/bioinformatics/btm356
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow Supplementary data
Right arrow All Versions of this Article:
23/18/2491    most recent
btm356v2
btm356v1
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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Chung, J.-L.
Right arrow Articles by Bourne, P. E
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chung, J.-L.
Right arrow Articles by Bourne, P. E
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author (2007). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Con-Struct Map: a Comparative Contact Map Analysis Tool

Jo-Lan Chung 1,2,3, John E Beaver 3, Eric D Scheeff 3,4 and Philip E Bourne 2,3,*

1Department of Chemistry and Biochemistry, 2Skaggs School of Pharmacy and Pharmaceutical Sciences, 3San Diego Supercomputer Center, University of California, San Diego, Gilman Drive, La Jolla, CA 92093, USA. 4Present address: Razavi-Newman Center for Bioinformatics, The Salk Institute for Biological Studies, 10010 North Torrey Pines Rd., La Jolla, CA 92037, USA

*To whom correspondence should be addressed. Philip E. Bourne, E-mail: pbourne{at}ucsd.edu


  Abstract

Summary: Con-Struct Map is a graphical tool for the comparative study of protein structures. The tool detects potential conserved residue contacts shared by multiple protein structures by superimposing their contact maps according to a multiple structure alignment. In general, Con-Struct Map allows the study of structural changes resulting from, for example, sequence substitutions, or alternatively, the study of conserved components of a structure framework across structurally aligned proteins. Specific applications include the study of sequence-structure relationship in distantly related proteins and the comparisons of wild type and mutated proteins.

Availability: http://pdbrs3.sdsc.edu/ConStructMap/viewer_argument_generator/singleArguments

Contact: pbourne{at}ucsd.edu

Associate Editor: Prof. Alsonso Valencia

Received on May 11, 2007; revised on July 1, 2007; accepted on July 3, 2007

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
H. K. Ho, M. J. Kuiper, and R. Kotagiri
PConPy--a Python module for generating 2D protein maps
Bioinformatics, December 15, 2008; 24(24): 2934 - 2935.
[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.