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Nucleic Acids Res. 2010 Jul;38(Web Server issue):W450-6. doi: 10.1093/nar/gkq328. Epub 2010 Apr 30.

ConPlex: a server for the evolutionary conservation analysis of protein complex structures.

Author information

1
School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea.

Abstract

Evolutionary conservation analyses are important for the identification of protein-protein interactions. For protein complex structures, sequence conservation has been applied to determine protein oligomerization states, to characterize native interfaces from non-specific crystal contacts, and to discriminate near-native structures from docking artifacts. However, a user-friendly web-based service for evolutionary conservation analysis of protein complexes has not been available. Therefore, we developed ConPlex (http://sbi.postech.ac.kr/ConPlex/) a web application that enables evolutionary conservation analyses of protein interactions within protein quaternary structures. Users provide protein complex structures; ConPlex automatically identifies protein interfaces and carries out evolutionary conservation analyses for the interface regions. Moreover, ConPlex allows the results of the residue-specific conservation analysis to be displayed on the protein complex structure and provides several options to customize the display output to fit each user's needs. We believe that ConPlex offers a convenient platform to analyze protein complex structures based on evolutionary conservation of protein-protein interface residues.

PMID:
20435678
PMCID:
PMC2896159
DOI:
10.1093/nar/gkq328
[Indexed for MEDLINE]
Free PMC Article

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