Arbitrary protein-protein docking targets biologically relevant interfaces.

ABSTRACT:

Background

Protein-protein recognition is of fundamental importance in the vast majority of biological processes. However, it has already been demonstrated that it is very hard to distinguish true complexes from false complexes in so-called cross-docking experiments, where binary protein complexes are separated and the isolated proteins are all docked against each other and scored. Does this result, at least in part, reflect a physical reality? False complexes could reflect possible nonspecific or weak associations.

Results

In this paper, we investigate the twilight zone of protein-protein interactions, building on an interesting outcome of cross-docking experiments: false complexes seem to favor residues from the true interaction site, suggesting that randomly chosen partne

SUBMITTER: Martin J 

PROVIDER: S-EPMC3441232 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature