Efficient flexible backbone protein-protein docking for challenging targets.

ABSTRACT:

Motivation

Binding-induced conformational changes challenge current computational docking algorithms by exponentially increasing the conformational space to be explored. To restrict this search to relevant space, some computational docking algorithms exploit the inherent flexibility of the protein monomers to simulate conformational selection from pre-generated ensembles. As the ensemble size expands with increased flexibility, these methods struggle with efficiency and high false positive rates.

Results

Here, we develop and benchmark RosettaDock 4.0, which efficiently samples large conformational ensembles of flexible proteins and docks them using a novel, six-dimensional, coarse-grained score function. A strong discriminative ability allows an eight-fold higher enrichment

SUBMITTER: Marze NA 

PROVIDER: S-EPMC6184633 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature