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MobiDB: a comprehensive database of intrinsic protein disorder annotations
Tomás Di Domenico1, Ian Walsh, Alberto J M Martin
1Department of Biology, University of Padova, Viale G. Colombo 3, 35131 Padova, Italy.
Bioinformatics (Oxford, England)
|June 5, 2012
Summary
MobiDB centralizes protein disorder data from DisProt, PDB, and NMR structures, plus predictions. It classifies disorder into flexible and constrained types, offering a comprehensive resource for researchers.
Area of Science:
- Structural biology
- Bioinformatics
- Proteomics
Background:
- Disordered protein regions are crucial for biological functions.
- Existing disorder databases like DisProt are limited in scope.
- Protein Data Bank (PDB) offers some disorder insights from missing residues in X-ray structures.
Purpose of the Study:
- To create a centralized, comprehensive database for protein disorder information.
- To expand upon existing disorder data sources.
- To classify disordered regions into flexible and constrained types.
Main Methods:
- Integrated data from DisProt, PDB (X-ray and NMR structures).
- Incorporated predictions from ESpritz and IUpred disorder predictors.
- Developed a weighted consensus approach for disorder classification.
- Established a user submission system for manual annotations.
Main Results:
- MobiDB provides experimental annotations for 17,285 proteins.
- Annotated 565,200 sequences from the SwissProt database using predictions.
- Classified disordered regions into flexible and constrained categories.
- 6-20% of residues predicted as disordered, varying by prediction method.
Conclusions:
- MobiDB serves as a valuable, expanded resource for protein disorder data.
- The database facilitates the study of protein function and biological roles.
- Offers a unified view of experimental and predicted disorder information.
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