DisProt: the Database of Disordered Proteins
Indiana University School of Medicine · Indiana University – Purdue University Indianapolis · +5 more institutions
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…
Citation impact
- FWCI
- 14.86
- Percentile
- 100%
- References
- 47
Authors
12- MDMegan D. SickmeierCorresponding
Indiana University School of Medicine, Indiana University – Purdue University Indianapolis
- JAJohn A. Hamilton
Indiana University School of Medicine, Indiana University – Purdue University Indianapolis
- TLTanguy LeGall
Indiana University School of Medicine, Indiana University – Purdue University Indianapolis
- VVVladimir Vacic
University of California, Riverside
- MSMarc S. Cortese
Indiana University School of Medicine, Indiana University – Purdue University Indianapolis
Topics & keywords
- Intrinsically disordered proteins
- Biology
- Computational biology
- Function (biology)
- Protein structure
- Protein function
- Database
- Genetics