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Biological Function
Caspase-6 is a member of the Cysteine-Aspartic protease family, and involved in apoptosis. It is most notably involved in neurodegenerative diseases, such as Alzheimer's disease and dementia.
Structural Overview
Inactive State
When the protein is in the inactive state it is a Homotetramer.
Active State
Originally it was thought to be cleaved and activated by a combination of Caspases-3 and -7, but research has shown that Caspase-6 enters the active state by self-cleaving at residue 193 after a sequence of TEVD. The protein then becomes a Tetramer of Dimers.
this shows the protein bound
Mechanism of Action
Mechanism is unknown as of right now. The active sight is known to be HIS-121, CYS-163, and GLU-174. It is tightly regulated by Zinc binding to an allosteric site.
Zinc Ligand(s)
The Zinc ligand is known to inhibit the Caspase-6 protein.
Other Ligands
Other ligands that bind to Caspase-6 are caspase-8, which is activated within the caspase-chain by Caspase 6. After it being activated by Caspase-6, Caspase-8 is then in it's active state. Caspase-6 has been know to be a self-activator, so other Caspase-6 proteins are also known to be ligands that are bound at the active site.
