Structural assembly of two-domain proteins by rigid-body docking.

ABSTRACT:

Background

Modelling proteins with multiple domains is one of the central challenges in Structural Biology. Although homology modelling has successfully been applied for prediction of protein structures, very often domain-domain interactions cannot be inferred from the structures of homologues and their prediction requires ab initio methods. Here we present a new structural prediction approach for modelling two-domain proteins based on rigid-body domain-domain docking.

Results

Here we focus on interacting domain pairs that are part of the same peptide chain and thus have an inter-domain peptide region (so called linker). We have developed a method called pyDockTET (tethered-docking), which uses rigid-body docking to generate domain-domain poses that are further scored by bin

SUBMITTER: Cheng TM 

PROVIDER: S-EPMC2579442 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature