MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins.

TitleMobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins.
Publication TypeJournal Article
Year of Publication2018
AuthorsPiovesan, D., F. Tabaro, L. Paladin, M. Necci, I. Mičetić, C. Camilloni, N. Davey, Z. Dosztányi, B. Mészáros, A. M. Monzon, G. Parisi, E. Schad, P. Sormanni, P. Tompa, M. Vendruscolo, W. F. Vranken, and S. C. E. Tosatto
JournalNucleic Acids Res
Volume46
IssueD1
PaginationD471-D476
Date Published2018 Jan 04
ISSN1362-4962
Abstract

The MobiDB (URL: mobidb.bio.unipd.it) database of protein disorder and mobility annotations has been significantly updated and upgraded since its last major renewal in 2014. Several curated datasets for intrinsic disorder and folding upon binding have been integrated from specialized databases. The indirect evidence has also been expanded to better capture information available in the PDB, such as high temperature residues in X-ray structures and overall conformational diversity. Novel nuclear magnetic resonance chemical shift data provides an additional experimental information layer on conformational dynamics. Predictions have been expanded to provide new types of annotation on backbone rigidity, secondary structure preference and disordered binding regions. MobiDB 3.0 contains information for the complete UniProt protein set and synchronization has been improved by covering all UniParc sequences. An advanced search function allows the creation of a wide array of custom-made datasets for download and further analysis. A large amount of information and cross-links to more specialized databases are intended to make MobiDB the central resource for the scientific community working on protein intrinsic disorder and mobility.

DOI10.1093/nar/gkx1071
Alternate JournalNucleic Acids Res.
PubMed ID29136219
PubMed Central IDPMC5753340
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