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IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.
Satoshi Fukuchi1, Shigetaka Sakamoto, Yukiko Nobe
1Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan. sfukuchi@maebashi-it.ac.jp
Nucleic Acids Research
|November 10, 2011
Summary
The IDEAL database curates knowledge on intrinsically disordered proteins, detailing their regions, interactions, and modifications. This resource aids in understanding protein function and molecular recognition.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioinformatics
Background:
- Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes but lack stable structures.
- Understanding the functional regions and properties of IDPs is essential for deciphering their biological significance.
Purpose of the Study:
- To introduce IDEAL, a comprehensive knowledgebase for experimentally verified intrinsically disordered proteins.
- To provide detailed annotations on IDPs, including disordered regions, interaction sites, and post-translational modifications.
Main Methods:
- Manual curation of literature and experimental data.
- Development of a user-friendly graphical interface and a computer-friendly XML format for data access.
Main Results:
- IDEAL compiles extensive annotations on intrinsically disordered regions, interaction sites, and post-translational modifications for numerous IDPs.
- The database explicitly identifies protean segments capable of transitioning between disordered and ordered states.
- Data is accessible through both graphical and XML formats.
Conclusions:
- IDEAL serves as a valuable data resource for researchers studying the functional regions of intrinsically disordered proteins.
- The curated information facilitates the study of molecular recognition mediated by IDPs.
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The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
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Overview