MobiDB: a comprehensive database of intrinsic protein disorder annotations

• DOI: 10.1093/bioinformatics/bts327
• Publication Date: 2012-06-04T14:09:02Z
• Authors: Tomás Di Domenico; Ian Walsh; Alberto J.M. Martin; Silvio C.E. Tosatto
• Keywords: User-Computer Interface; 0303 health sciences; 03 medical and health sciences; Magnetic Resonance Spectroscopy; Sequence Analysis, Protein; Proteins; Molecular Sequence Annotation; Crystallography, X-Ray; Databases, Protein; Protein Structure, Tertiary; 3. Good health

Abstract Motivation: Disordered protein regions are key to the function of numerous processes within an organism and to the determination of a protein's biological role. The most common source for protein disorder annotations, DisProt, covers only a fraction of the available sequences. Alternatively, the Protein Data Bank (PDB) has been mined for missing residues in X-ray crystallographic structures. Herein, we provide a centralized source for data on different flavours of disorder in protein structures, MobiDB, building on and expanding the content provided by already existing sources. In addition to the DisProt and PDB X-ray structures, we have added experimental information from NMR structures and five different flavours of two disorder predictors (ESpritz and IUpred). These are combined into a weighted consensus disorder used to classify disordered regions into flexible and constrained disorder. Users are encouraged to submit manual annotations through a submission form. MobiDB features experimental annotations for 17 285 proteins, covering the entire PDB and predictions for the SwissProt database, with 565 200 annotated sequences. Depending on the disorder flavour, 6–20% of the residues are predicted as disordered. Availability: The database is freely available at http://mobidb.bio.unipd.it/. Contact: [e-mail]