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Nucleic Acids Res. 2018 Jan 4;46(D1):D471-D476. doi: 10.1093/nar/gkx1071.

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

Author information

1
Department of Biomedical Sciences, University of Padua, via U. Bassi 58/b, 35131 Padua, Italy.
2
Institute of Biosciences and Medical Technology, Arvo Ylpön katu 34, 33520 Tampere, Finland.
3
Department of Agricultural Sciences, University of Udine, via Palladio 8, 33100 Udine, Italy.
4
Fondazione Edmund Mach, Via E. Mach 1, 38010 S. Michele all'Adige, Italy.
5
Department of Biosciences, University of Milan, 20133 Milano, Italy.
6
Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland.
7
UCD School of Medicine & Medical Science, University College Dublin, Belfield, Dublin 4, Ireland.
8
MTA-ELTE Lendület Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, 1/c Pázmány Péter sétány, H-1117, Budapest, Hungary.
9
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary.
10
Structural Bioinformatics Group, Department of Science and Technology, National University of Quilmes, CONICET, Roque Saenz Pena 182, Bernal B1876BXD, Argentina.
11
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
12
Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels 1050, Belgium.
13
VIB-VUB Center for Structural Biology, Flanders Institute for Biotechnology (VIB), Brussels 1050, Belgium.
14
Interuniversity Institute of Bioinformatics in Brussels, ULB/VUB, 1050 Brussels, Belgium.
15
CNR Institute of Neuroscience, via U. Bassi 58/b, 35131 Padua, Italy.

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.

PMID:
29136219
PMCID:
PMC5753340
DOI:
10.1093/nar/gkx1071
[Indexed for MEDLINE]
Free PMC Article

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