Flexible Backbone Assembly and Refinement of Symmetrical Homomeric Complexes.

ABSTRACT: Symmetrical homomeric proteins are ubiquitous in every domain of life, and information about their structure is essential to decipher function. The size of these complexes often makes them intractable to high-resolution structure determination experiments. Computational docking algorithms offer a promising alternative for modeling large complexes with arbitrary symmetry. Accuracy of existing algorithms, however, is limited by backbone inaccuracies when using homology-modeled monomers. Here, we present Rosetta SymDock2 with a broad search of symmetrical conformational space using a six-dimensional coarse-grained score function followed by an all-atom flexible-backbone refinement, which we demonstrate to be essential for physically realistic modeling of tightly packed complexes. In global do

SUBMITTER: Roy Burman SS 

PROVIDER: S-EPMC6719319 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature