Sandox Bay Serrano

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</StructureSection>
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<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''>
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<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'''
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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.
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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. 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>

Caspase-3 dimer (PDB entry 2h5i)

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Proteopedia Page Contributors and Editors (what is this?)

Banyuhay P. Serrano, Michal Harel

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