Sandbox Reserved 433
From Proteopedia
| Line 32: | Line 32: | ||
===Additional Features=== | ===Additional Features=== | ||
| + | -Role in apoptosis | ||
| + | --How it is activated (green scene of activation ligand?) | ||
| + | --catalytic site (if binding interactions doesn't cover this) | ||
| + | -Potential role in stem-cell differentiation: | ||
| + | "rather than by simply limiting self-renewal. In this model, caspase-3 may simultaneously engage factors to promote the gene expression profile and resulting phenotypic changes that result in a specific differentiated cell type" (Abdul-Ghani and Megeney 515) | ||
===Credits=== | ===Credits=== | ||
| Line 45: | Line 50: | ||
===References=== | ===References=== | ||
<references/> | <references/> | ||
| + | |||
| + | ''Rehabilitation of a Contract Killer: Caspase-3 Directs Stem Cell Differentiation.'' Mohammad Abdul-Ghani,Lynn A. Megeney [http://dx.doi.org/10.1016%2Fj.stem.2008.05.013] | ||
Revision as of 06:14, 5 March 2012
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Contents |
Caspase 3- 1rhk
Introduction
Caspases are a group of dimeric cysteine proteases that play important roles to control the ultimate steps of apoptosis and innate inflammation; they are also very important in cellular development, homeostasis and in a wide range of diseases such as neurodegeneration, ischemia and cancers. During apoptosis, the upstream initiator caspases, caspases 8 and 9, activate with the downstream executioner caspases, caspases 3, 6 and 7, via zymogen maturation. The activated executioner caspases then cleave upwards of 500 key proteins and DNA, which finally cause the death of cells. [1] Caspases 3 is one of the downstream executioner caspases which interacts with caspase 8 and 9. It is formed from a 32 kDa zymogen that is cleaved into 17 kDa and 12 kDa subunits. Caspase 3 has many of the typical characteristics which all currently-known caspases also own. For instance, its active site contains acysteine residue (Cys-285) and histidine residue (His-237) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence. [2] Besides apoptosis, caspase 3 also has many biological functions, such as normal brain development and several significant diseases including Alzheimer’s disease, Polycystic Kidney Disease [3] and Cancers.
Overall Structure
|
Binding Interactions
-Focus on difficulties in finding good inhibitors
-Chemical and conformational changes applied to various inhibitors
-Good drug candidates for inhibition
Binding sites for .
Additional Features
-Role in apoptosis
--How it is activated (green scene of activation ligand?) --catalytic site (if binding interactions doesn't cover this)
-Potential role in stem-cell differentiation:
"rather than by simply limiting self-renewal. In this model, caspase-3 may simultaneously engage factors to promote the gene expression profile and resulting phenotypic changes that result in a specific differentiated cell type" (Abdul-Ghani and Megeney 515)
Credits
Introduction - Di Lin
Overall Structure - Austin Virtue
Drug Binding Site - Jill Moore
Additional Features - Alex Way
References
Rehabilitation of a Contract Killer: Caspase-3 Directs Stem Cell Differentiation. Mohammad Abdul-Ghani,Lynn A. Megeney [1]
