DisProt: the Database of Disordered Proteins
Top Cited Papers
Open Access
- 1 December 2006
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 35 (Database) , D786-D793
- https://doi.org/10.1093/nar/gkl893
Abstract
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 Author Webpage.Keywords
This publication has 34 references indexed in Scilit:
- Insights into protein structure and function from disorder–complexity spaceProteins-Structure Function and Bioinformatics, 2006
- Unstructured Conformations Are a Substrate Requirement for the Sir2 Family of NAD-dependent Protein DeacetylasesJournal of Biological Chemistry, 2005
- Assessment of disorder predictions in CASP6Proteins-Structure Function and Bioinformatics, 2005
- Assessment of fold recognition predictions in CASP6Proteins-Structure Function and Bioinformatics, 2005
- Linear motifs: Evolutionary interaction switchesFEBS Letters, 2005
- Glycoprotein‐specific ubiquitin ligases recognize N‐glycans in unfolded substratesEMBO Reports, 2005
- The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfoldedFEBS Letters, 2002
- Signaling Through Scaffold, Anchoring, and Adaptor ProteinsScience, 1997
- An Exploration of the Effects of Constraints on the Phosphorylation of Synthetic Protein Tyrosine Kinase Peptide SubstratesJournal of Peptide Science, 1996
- Protein structure and enzyme action.1958