Reuse of structural domain-domain interactions in protein networks

Background: Protein interactions are thought to be largely mediated by interactions between structural domains. Databases such as iPfam relate interactions in protein structures to known domain families. Here, we investigate how the domain interactions from the iPfam database are distributed in protein interactions taken from the HPRD, MPact, BioGRID, DIP and IntAct databases. Results: We find that known structural domain interactions can only explain a subset of 4–19% of the available protein interactions, nevertheless this fraction is still significantly bigger than expected by chance. There is a correlation between the frequency of a domain interaction and the connectivity of the proteins it occurs in. Furthermore, a large proportion of protein interactions can be attributed to a small number of domain interactions. We conclude that many, but not all, domain interactions constitute reusable modules of molecular recognition. A substantial proportion of domain interactions are cons...

• Type: Journal
• Year: 2007
• Where: BMCBI
• Authors: Benjamin Schuster-Böckler, Alex Bateman
• Keywords: BMCBI 2007, Domain Interactions, Protein Interactions, Structural Domain