MobiDB


NAR Molecular Biology Database Collection entry number 72
mobidb.bio.unipd.it
Damiano Piovesan 1, Francesco Tabaro 1,2 , Lisanna Paladin 1 , Marco Necci 1,3,4 , Ivan Micetic 1 , Carlo Camilloni 5 , Norman Davey 6,7 , Zsuzsanna Dosztányi 8 , Balint Meszaros 8,9 , Alexander Miguel Monzon 10 , Gustavo Parisi 10 , Eva Schad 9 , Pietro Sormanni 11 , Peter Tompa 9,12,13 , Michele Vendruscolo 11 , Wim F. Vranken 12,13,14 and Silvio C.E. Tosatto 1,15
1. Dept. 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 Dept. 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 Dipartimento di Bioscienze, Università degli Studi di Milano, 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, 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, United Kingdom
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.

Database Description

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.

Acknowledgements

The work was supported by COST Action BM1405 NGP-net. We also acknowledge ELIXIR-IIB(elixir- italy.org), the Italian Node of the European ELIXIR infrastructure (elixir-europe.org), for supporting the development and maintenance of MobiDB. DP is an AIRC research fellow. ZD acknowledges support from the Hungarian Academy of Sciences “Lendület” Grant (LP201418/2016) and the Hungarian Scientific Research Fund (OTKA K 108798). BM holds a postdoctoral fellowship of the Hungarian Academy of Sciences. GP is supported by Agencia de Ciencia y Tecnología (PICT-2014- 3430) and Universidad Nacional de Quilmes (1402/15). ES acknowledges the support of OTKA grant PD-OTKA 108772. PT is supported by the Odysseus grant G.0029.12 from Research Foundation Flanders (FWO). WFV is supported by the FWO project G032816N. Part of the work was supported by AIRC IG grant 17753 to ST.


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