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User:Loganne Wertz/Sandbox1
From Proteopedia
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| - | ==Caspase-6 in ''Homo sapiens''== | + | == '''Caspase-6 in ''Homo sapiens''''' == |
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<StructureSection load='4FXO' size='340' side='right' caption='Caspase-6' scene=''> | <StructureSection load='4FXO' size='340' side='right' caption='Caspase-6' scene=''> | ||
| - | + | Found at high concentrations in the brain and bordering tissues, Caspase-6 has been implicated in several neurological diseases including Alzheimer's and dementia. It's primarily involved in apoptosis through a largely ambiguous mechanism. It is classified as an [https://en.wikipedia.org/wiki/Endopeptidase]endopeptidase as it cleaves an internal peptide bond of its substrate. It has relatively low specificity in the binding site which allows for a variety of substrates, including other caspase enzymes to bind. Furthermore, it is a part of the cysteine aspartate family, which have these critical amino acid residues in the active site of the enzyme. Caspase-6 has both an inactive zinc-bound conformation and an active ligand-bound conformation, which are largely regulated by variations in zinc concentration. | |
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[[Image:Caspase-6 protein.jpg|100 px|left|thumb|Figure Legend]] | [[Image:Caspase-6 protein.jpg|100 px|left|thumb|Figure Legend]] | ||
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== Structure == | == Structure == | ||
| - | :Active Site | + | :'''Active Site''' |
| - | :Zinc Exosite | + | :'''Zinc Exosite''' |
== Inhibition == | == Inhibition == | ||
| + | :'''Zinc Inhibition''' | ||
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| + | :'''Phosphorylation''' | ||
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| + | :'''Zymogen Activation''' | ||
== Relevance == | == Relevance == | ||
Revision as of 12:46, 28 March 2017
Caspase-6 in Homo sapiens
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