Association rate constants of ras-effector interactions are evolutionarily conserved.

ABSTRACT: Evolutionary conservation of protein interaction properties has been shown to be a valuable indication for functional importance. Here we use homology interface modeling of 10 Ras-effector complexes by selecting ortholog proteins from 12 organisms representing the major eukaryotic branches, except plants. We find that with increasing divergence time the sequence similarity decreases with respect to the human protein, but the affinities and association rate constants are conserved as predicted by the protein design algorithm, FoldX. In parallel we have done computer simulations on a minimal network based on Ras-effector interactions, and our results indicate that in the absence of negative feedback, changes in kinetics that result in similar binding constants have strong consequences on net

SUBMITTER: Kiel C 

PROVIDER: S-EPMC2588540 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature