Abstract:

Background: Recently, there has been much interest in relating domain-domain interactions ( DDIs) to protein-protein interactions ( PPIs) and vice versa, in an attempt to understand the molecular basis of PPIs. Results: Here we map structurally derived DDIs onto the cellular PPI networks of different organisms and demonstrate that there is a catalog of domain pairs that is used to mediate various interactions in the cell. We show that these DDIs occur frequently in protein complexes and that homotypic interactions ( of a domain with itself) are abundant. A comparison of the repertoires of DDIs in the networks of Escherichia coli, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, and Homo sapiens shows that many DDIs are evolutionarily conserved. Conclusion: Our results indicate that different organisms use the same `building blocks' for PPIs, suggesting that the functionality of many domain pairs in mediating protein interactions is maintained in evolution.

Website

DOI:

10.1186/gb-2006-7-12-r125