User:Loganne Wertz/Sandbox1

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==Caspase-6 in ''Homo sapiens''== 2
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== '''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=''>
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This is a default text for your page '''Loganne Wertz/Sandbox1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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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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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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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 ==
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:Active Site
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:'''Active Site'''
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:Zinc Exosite
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:'''Zinc Exosite'''
== Inhibition ==
== Inhibition ==
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:'''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

Caspase-6

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References

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