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===Introduction=== | ===Introduction=== | ||
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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 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] | 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] | ||
Revision as of 05:23, 5 March 2012
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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
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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
Credits
Introduction - Di Lin
Overall Structure - Austin Virtue
Drug Binding Site - Jill Moore
Additional Features - name of team member
