Sandbox Reserved 1061

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Revision as of 12:46, 14 March 2017

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This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.

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Human Caspase-6

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Biological Function
2 Structural Overview
- 2.1 Inactive State
- 2.2 Active State
3 Mechanism of Action
4 Zinc Ligand(s)
5 Other Ligands

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

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.

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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

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.

References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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Sandbox Reserved 1061

From Proteopedia

Revision as of 12:46, 14 March 2017

Human Caspase-6

Contents

Biological Function

Structural Overview

Inactive State

Active State

Mechanism of Action

Zinc Ligand(s)

Other Ligands

References

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 The Zinc ligand is known to inhibit the
 == Other Ligands ==
-Other ligands that bind to Caspase-6 are caspase-8, which is activated within the caspase-chain by Caspase 6.
+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.
 </StructureSection>