Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis.

ABSTRACT: Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in a host response and parasite survival. Thus, these proteins are interesting molecular targets for vaccine and drug development. Here, we have determined two crystal structures of the calmodulin like domain (amino acid [aa] positions 1-81) and dynein light chain (DLC)-like domain (aa 83-177) of a 20.8-kDa tegumental-allergen-like protein from Clonorchis sinensis (CsTAL3). The calmodulin like domain has two Ca²⁺-binding sites (named CB1 and CB2), but Ca²⁺ binds to only one site, CB1. The DLC-like domain has a dimeric conformation; the interface is formed mainly by hydrogen bond

SUBMITTER: Jo CH 

PROVIDER: S-EPMC5431922 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature