Reuse of Domain Interactions in Protein Networks
Author Information
Author(s): Schuster-Böckler Benjamin, Bateman Alex
Primary Institution: Wellcome Trust Sanger Institute
Hypothesis
How are domain interactions from the iPfam database distributed in protein interactions from various databases?
Conclusion
Many domain interactions are reusable modules of molecular recognition, but the number of known interactions is limited.
Supporting Evidence
- Known structural domain interactions explain only 4-19% of available protein interactions.
- A significant portion of domain interactions are conserved across species.
- The study found a correlation between the frequency of domain interactions and protein connectivity.
Takeaway
This study looks at how parts of proteins interact with each other and finds that some of these interactions are used over and over again in different proteins.
Methodology
The study analyzed protein interactions from five major databases and compared them to known domain interactions from the iPfam database.
Potential Biases
The selection of protein complexes in the PDB database is biased, affecting the assessment of domain interactions.
Limitations
The study is limited by the small number of available protein structures and the low coverage of iPfam domain pairs in experimental interactions.
Participant Demographics
The study includes protein interactions from five species: E. coli, S. cerevisiae, C. elegans, D. melanogaster, and H. sapiens.
Statistical Information
P-Value
p<0.000001
Statistical Significance
p<0.000001
Digital Object Identifier (DOI)
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