Conservation of Intrinsic Disorder in Protein Domains and Families: I. A Database of Conserved Predicted Disordered Regions
Document Type
Article
Publication Date
2006
Keywords
Intrinsic Disorder, Protein Structure−function, Disorder Prediction, PONDR
Digital Object Identifier (DOI)
https://doi.org/10.1021/pr060048x
Abstract
Many protein regions have been shown to be intrinsically disordered, lacking unique structure under physiological conditions. These intrinsically disordered regions are not only very common in proteomes, but also crucial to the function of many proteins, especially those involved in signaling, recognition, and regulation. The goal of this work was to identify the prevalence, characteristics, and functions of conserved disordered regions within protein domains and families. A database was created to store the amino acid sequences of nearly one million proteins and their domain matches from the InterPro database, a resource integrating eight different protein family and domain databases. Disorder prediction was performed on these protein sequences. Regions of sequence corresponding to domains were aligned using a multiple sequence alignment tool. From this initial information, regions of conserved predicted disorder were found within the domains. The methodology for this search consisted of finding regions of consecutive positions in the multiple sequence alignments in which a 90% or more of the sequences were predicted to be disordered. This procedure was constrained to find such regions of conserved disorder prediction that were at least 20 amino acids in length. The results of this work included 3653 regions of conserved disorder prediction, found within 2898 distinct InterPro entries. Most regions of conserved predicted disorder detected were short, with less than 10% of those found exceeding 30 residues in length.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Journal of Proteome Research, v. 5, issue 4, p. 879-887
Scholar Commons Citation
Chen, Jessica Walton; Romero, Pedro R.; Uversky, Vladimir N.; and Dunker, A. Keith, "Conservation of Intrinsic Disorder in Protein Domains and Families: I. A Database of Conserved Predicted Disordered Regions" (2006). Molecular Medicine Faculty Publications. 756.
https://digitalcommons.usf.edu/mme_facpub/756
