Spatial chemical conservation of hot spot interactions in protein-protein complexes.

ABSTRACT:

Background

Conservation of the spatial binding organizations at the level of physico-chemical interactions is important for the formation and stability of protein-protein complexes as well as protein and drug design. Due to the lack of computational tools for recognition of spatial patterns of interactions shared by a set of protein-protein complexes, the conservation of such interactions has not been addressed previously.

Results

We performed extensive spatial comparisons of physico-chemical interactions common to different types of protein-protein complexes. We observed that 80% of these interactions correspond to known hot spots. Moreover, we show that spatially conserved interactions allow prediction of hot spots with a success rate higher than obtained by methods based

SUBMITTER: Shulman-Peleg A 

PROVIDER: S-EPMC2231411 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature