Sandox Bay Serrano
From Proteopedia
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Caspases are synthesized in the cell in their zymogen forms, consisting of an N-terminal prodomain followed by a large and a small subunit linked to each other by an intersubunit linker. As an executioner caspase, caspase-3 has a short N-terminal prodomain and like any other caspases, cleavage of the intersubunit linker at a specific aspartate residue generates the mature form of the enzyme. | Caspases are synthesized in the cell in their zymogen forms, consisting of an N-terminal prodomain followed by a large and a small subunit linked to each other by an intersubunit linker. As an executioner caspase, caspase-3 has a short N-terminal prodomain and like any other caspases, cleavage of the intersubunit linker at a specific aspartate residue generates the mature form of the enzyme. | ||
| - | + | <Structure load=''Sandox_Bay_Serrano/Dimer05/1'>TextToBeDisplayed</scene>' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |
</StructureSection> | </StructureSection> | ||
| - | <StructureSection load='2h5i_mm1-1.pdb' size='350' side='right' caption='Caspase-3 dimer (PDB entry [[2h5i]])' scene='Sandox_Bay_Serrano/ | + | The <StructureSection load='2h5i_mm1-1.pdb' size='350' side='right' caption='Caspase-3 dimer (PDB entry [[2h5i]])' scene='Sandox_Bay_Serrano/Dimer03/1'></scene>''> |
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Anything in this section will appear adjacent to the 3D structure and will be scrollable. | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
Revision as of 17:58, 12 December 2012
Introduction
Caspase-3 Structure
Caspases are synthesized in the cell in their zymogen forms, consisting of an N-terminal prodomain followed by a large and a small subunit linked to each other by an intersubunit linker. As an executioner caspase, caspase-3 has a short N-terminal prodomain and like any other caspases, cleavage of the intersubunit linker at a specific aspartate residue generates the mature form of the enzyme.
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