Caspase-6 Undergoes a Distinct Helix-Strand Interconversion upon Substrate Binding.

ABSTRACT: Caspases are cysteine aspartate proteases that are major players in key cellular processes, including apoptosis and inflammation. Specifically, caspase-6 has also been implicated in playing a unique and critical role in neurodegeneration; however, structural similarities between caspase-6 and other caspase active sites have hampered precise targeting of caspase-6. All caspases can exist in a canonical conformation, in which the substrate binds atop a β-strand platform in the 130's region. This caspase-6 region can also adopt a helical conformation that has not been seen in any other caspases. Understanding the dynamics and interconversion between the helical and strand conformations in caspase-6 is critical to fully assess its unique function and regulation. Here, hydrogen/deuterium exchan

SUBMITTER: Dagbay KB 

PROVIDER: S-EPMC5377803 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature