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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. | 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. | ||
{{STRUCTURE_1f1j | PDB=1f1j | SCENE= }} | |||
==Active Site== | ==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. | 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. | ||
Revision as of 15:25, 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 7Caspase 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 SiteActive 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.