Unraveling the structural landscape of intra-chain domain interfaces: Implication in the evolution of domain-domain interactions.

ABSTRACT: Intra-chain domain interactions are known to play a significant role in the function and stability of multidomain proteins. These interactions are mediated through a physical interaction at domain-domain interfaces (DDIs). With a motivation to understand evolution of interfaces, we have investigated similarities among DDIs. Even though interfaces of protein-protein interactions (PPIs) have been previously studied by structurally aligning interfaces, similar analyses have not yet been performed on DDIs of either multidomain proteins or PPIs. For studying the structural landscape of DDIs, we have used iAlign to structurally align intra-chain domain interfaces of domains. The interface alignment of spatially constrained domains (due to inter-domain linkers) showed that ~88% of these could ide

SUBMITTER: Verma R 

PROVIDER: S-EPMC6677297 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature