Sandox Bay Serrano
From Proteopedia
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</StructureSection> | </StructureSection> | ||
- | + | <StructureSection load='2h5i_mm1-1.pdb' size='350' side='right' caption='Caspase-3 dimer (PDB entry [[2h5i]])' scene='Sandox_Bay_Serrano/Scene01_dimer/1'>dimeric</scene''> | |
- | <StructureSection load='2h5i_mm1-1.pdb' size='350' side='right' caption='Caspase-3 dimer (PDB entry [[2h5i]])' scene='Sandox_Bay_Serrano/Scene01_dimer/1'> | + | |
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'''Caspase-3 Structure''' | '''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. | + | 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. Caspase-3 in its functional form is <scene name='Sandox_Bay_Serrano/Scene01_dimer/1'>dimeric</scene>, with the dimer interface being stabilized by interactions between the small subunits of each monomer. Binding of a <scene name='Sandox_Bay_Serrano/Scene01_substrate/2'>substrate</scene>, such as DEVD-CHO to the active site of the enzyme induces a conformational change that allows the L2 and L2' loops to interlock and stabilize the active site. |
Revision as of 18:27, 12 December 2012
Introduction
</StructureSection>
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