Sandbox88
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The active site for Caspase 7 takes full advantage of acid base chemistry. Histidine 144 will act as a base, pulling the hydrogen away from cysteine 186. This will make that cysteine very nucleophilic and thus very active. It will bind substrate and cleave after an aspartate residue. | The active site for Caspase 7 takes full advantage of acid base chemistry. Histidine 144 will act as a base, pulling the hydrogen away from cysteine 186. This will make that cysteine very nucleophilic and thus very active. It will bind substrate and cleave after an aspartate residue. | ||
| - | + | <scene name='Sandbox88/Active_site/4'>Active Site</scene> | |
| - | <scene name=' | + | |
Revision as of 13:09, 13 April 2011
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This sandbox is in use until August 1, 2011 for UMass Chemistry 423. Others please do not edit this page. Thanks!
Caspase 7
This is the structure for Caspase 7 with substrate bound. Caspase 7 is a Cysteine dependent protease that cleaves after ASPartate residues. The substrate here is the peptide DEVD. Caspase 7 plays a critical role in apoptosis as an initiator that cleaves downstream targets.
All caspases are zymogens. In the case of Casp7, this means that there is a prodomain that, when attached, renders the protein inactive. However, this prodomain is easily cleaved off, thus activating Casp7 as a protease.
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| 1f1j, resolution 2.35Å () | |||||||
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| Ligands: | |||||||
| Non-Standard Residues: | , | ||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Active Site
The active site for Caspase 7 takes full advantage of acid base chemistry. Histidine 144 will act as a base, pulling the hydrogen away from cysteine 186. This will make that cysteine very nucleophilic and thus very active. It will bind substrate and cleave after an aspartate residue.
