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
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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.
Articles |
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
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Yu. Lobanov, B. A. Shoemaker, S. O. Garbuzynskiy, J. H. Fong, A. R. Panchenko, and O. V. Galzitskaya ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder Nucleic Acids Res., November 11, 2009; (2009) gkp963v1. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Rancurel, M. Khosravi, A. K. Dunker, P. R. Romero, and D. Karlin Overlapping Genes Produce Proteins with Unusual Sequence Properties and Offer Insight into De Novo Protein Creation J. Virol., October 15, 2009; 83(20): 10719 - 10736. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Tsvetkov, N. Reuven, C. Prives, and Y. Shaul Susceptibility of p53 Unstructured N Terminus to 20 S Proteasomal Degradation Programs the Stress Response J. Biol. Chem., September 25, 2009; 284(39): 26234 - 26242. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. N. Pace, G. R. Grimsley, and J. M. Scholtz Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility J. Biol. Chem., May 15, 2009; 284(20): 13285 - 13289. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Erales, S. Lignon, and B. Gontero CP12 from Chlamydomonas reinhardtii, a Permanent Specific "Chaperone-like" Protein of Glyceraldehyde-3-phosphate Dehydrogenase J. Biol. Chem., May 8, 2009; 284(19): 12735 - 12744. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 V. A. Money, H. K. McPhee, J. A. Mosely, J. M. Sanderson, and R. P. Yeo Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction PNAS, March 17, 2009; 106(11): 4441 - 4446. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. E. Davey, D. C. Shields, and R. J. Edwards Masking residues using context-specific evolutionary conservation significantly improves short linear motif discovery Bioinformatics, February 15, 2009; 25(4): 443 - 450. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Haaning, S. Radutoiu, S. V. Hoffmann, J. Dittmer, L. Giehm, D. E. Otzen, and J. Stougaard An Unusual Intrinsically Disordered Protein from the Model Legume Lotus japonicus Stabilizes Proteins in Vitro J. Biol. Chem., November 7, 2008; 283(45): 31142 - 31152. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. J. Bingham, E. Rudino-Pinera, N. A. G. Meenan, U. Schwarz-Linek, J. P. Turkenburg, M. Hook, E. F. Garman, and J. R. Potts Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains PNAS, August 26, 2008; 105(34): 12254 - 12258. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. W. Brandt, J. Heringa, and J. A. M. Leunissen SEQATOMS: a web tool for identifying missing regions in PDB in sequence context Nucleic Acids Res., July 1, 2008; 36(suppl_2): W255 - W259. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. M. Simon, F. J. R. Sousa, R. Mohana-Borges, and G. C. Walker Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products PNAS, January 29, 2008; 105(4): 1152 - 1157. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Raychaudhuri, M. Sinha, D. Mukhopadhyay, and N. P. Bhattacharyya HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity Hum. Mol. Genet., January 15, 2008; 17(2): 240 - 255. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Fuxreiter, P. Tompa, and I. Simon Local structural disorder imparts plasticity on linear motifs Bioinformatics, April 15, 2007; 23(8): 950 - 956. [Abstract] [Full Text] [PDF]
|
|