Binding properties and evolution of homodimers in protein-protein interaction networks.

ABSTRACT: We demonstrate that protein-protein interaction networks in several eukaryotic organisms contain significantly more self-interacting proteins than expected if such homodimers randomly appeared in the course of the evolution. We also show that on average homodimers have twice as many interaction partners than non-self-interacting proteins. More specifically, the likelihood of a protein to physically interact with itself was found to be proportional to the total number of its binding partners. These properties of dimers are in agreement with a phenomenological model, in which individual proteins differ from each other by the degree of their 'stickiness' or general propensity toward interaction with other proteins including oneself. A duplication of self-interacting proteins creates a pair of

SUBMITTER: Ispolatov I 

PROVIDER: S-EPMC1160523 | biostudies-literature | 2005

REPOSITORIES: biostudies-literature