Caspases from scleractinian coral show unique regulatory features
Suman Shrestha, Jessica Tung, Robert D. Grinshpon, Paul Swartz, Paul T. Hamilton, Bradford Dimos, Laura D. Mydlarz, A. Clay Clark
Abstract
Dase. The first X-ray crystal structure of a coral caspase, of PaCasp7a determined at 1.57 Å resolution, reveals a conserved fold and an N-terminal peptide bound near the active site that may serve as a regulatory exosite. The binding pocket has been observed in initiator caspases of other species. These results suggest mechanisms for the evolution of substrate selection while maintaining common activation mechanisms of CARD-mediated dimerization.
Topics & Concepts
CaspaseBiologyCoralCell biologyProgrammed cell deathApoptosisEcologyBiochemistryCoral and Marine Ecosystems StudiesAquaculture disease management and microbiotaVibrio bacteria research studies