Nucleic Acids Research Advance Access originally published online on December 1, 2006
Nucleic Acids Research 2007 35(Database issue):D786-D793; doi:10.1093/nar/gkl893
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Nucleic Acids Research, 2007, Vol. 35, Database issue D786-D793
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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DisProt: the Database of Disordered Proteins
1 Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine Indianapolis, IN 46202, USA 2 Computer Science and Engineering, University of California Riverside Riverside, CA 92521, USA 3 Institute of Enzymology, Biological Research Center Hungarian Academy of Sciences, Budapest, Hungary 4 School of Informatics, Indiana University Indianapolis, IN 46202, USA 5 Center for Information Science and Technology, Temple University Philadelphia, PA 19122, USA 6 Institute for Biological Instrumentation, Russian Academy of Sciences 142292 Pushchino, Moscow Region, Russia
*To whom correspondence should be addressed. Tel: +1 317 278 9650; Fax: +1 317 278 9217; Email: kedunker{at}iupui.edu
Received August 15, 2006. Revised October 5, 2006. Accepted October 10, 2006.
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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