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DOMMINO: a database of macromolecular interactions.
Xingyan Kuang1, Jing Ginger Han, Nan Zhao
1Informatics Institute and Department of Computer Science and Bond Life Science Center, University of Missouri, Columbia, MO 65211, USA.
Nucleic Acids Research
|December 3, 2011
Summary
DOMMINO is a new database cataloging macromolecular interactions, including protein domains and non-structured regions. It offers tools to visualize interaction networks and interface structures for comprehensive analysis.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Macromolecular complex structures reveal interactions mediated by domains and non-structured regions like linkers and terminal sequences.
- Existing databases may not fully capture the diversity of interaction interfaces in macromolecular complexes.
Purpose of the Study:
- To present DOMMINO, a comprehensive database of macromolecular interactions.
- To include interactions involving protein domains, interdomain linkers, N- and C-terminal regions, and protein peptides.
Main Methods:
- DOMMINO integrates SCOP domain annotations with SUPERFAMILY predictions.
- The database is automatically updated weekly.
- A three-stage pipeline facilitates interaction analysis: flexible search, interaction network visualization, and interface structure visualization.
Main Results:
- DOMMINO provides a comprehensive resource for studying macromolecular interactions.
- The database includes diverse interaction types beyond just protein domains.
- The user interface supports detailed analysis of interaction networks and specific interface structures.
Conclusions:
- DOMMINO enhances the study of macromolecular interactions by incorporating a wider range of interaction types.
- The database and its visualization tools offer valuable insights into the structural basis of molecular recognition.
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