Maureen E. Hill/Sandbox1

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The <scene name='56/566502/Active_site_conformation/1'>active site</scene> is made up of four flexible loops which include L2, L3 and L4 from one half of the dimer that interact with L2' from the opposite half of the dimer. In the <scene name='56/566502/Procaspase_zymogen/1'>procaspase-7 zymogen</scene>, the loops are disordered, which prevents substrate binding. Upon cleavage at the intersubunit linker, the active-site loop bundle becomes partially ordered, whereas L2' stays in the inactive, down conformation. At this point, caspase-7 may bind either substrate or allosteric inhibitors. <scene name='56/566502/Active_site_substrate/2'>Caspase-7 bound to suicide inhibitor/substrate mimic DEVD-CHO</scene> traps the protein an active/substrate bound conformation. Substrate binding forces L2' to move upward, creating a foundation beneath the L2 bundle.
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The <scene name='56/566502/Active_site_conformation/1'>active site</scene> is made up of four flexible loops which include L2, L3 and L4 from one half of the dimer that interact with L2' from the opposite half of the dimer. In the <scene name='56/566502/Procaspase_zymogen/1'>procaspase-7 zymogen</scene>, the loops are disordered, which prevents substrate binding. Upon cleavage at the intersubunit linker, the active-site loop bundle becomes partially ordered, whereas L2' stays in the inactive, down conformation. At this point, caspase-7 may bind either substrate or allosteric inhibitors. <scene name='56/566502/Active_site_substrate_color/1'>Caspase-7 bound to suicide inhibitor/substrate mimc DEVD-CHO</scene> traps the protein an active/substrate bound conformation. Substrate binding forces L2' to move upward, creating a foundation beneath the L2 bundle.

Revision as of 15:38, 3 December 2013

Executioner Caspase-7

Structure of caspase-7(PDB entry 1f1j)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Derek MacPherson, Maureen E. Hill

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