Molecular Playground/Executioner Caspase-7: Difference between revisions
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<scene name='56/566502/Dica_bound_caspase_7/2'>Caspase-7 bound to allosteric inhibitor DICA</scene> at the dimer interface. The mechanism of allosteric inhibition of DICA starts with binding to C290 within the dimer interface, this displaces Y223. The movement of tyrosine from the partially active state of the enzyme forces R187 into a position that both physically blocks substrate binding, as well as, move the active site cysteine 186. The resulting conformational changes inactivate the enzyme, making it unable to process substrate. | <scene name='56/566502/Dica_bound_caspase_7/2'>Caspase-7 bound to allosteric inhibitor DICA</scene> at the dimer interface. The mechanism of allosteric inhibition of DICA starts with binding to C290 within the dimer interface, this displaces Y223. The movement of tyrosine from the partially active state of the enzyme forces R187 into a position that both physically blocks substrate binding, as well as, move the active site cysteine 186. The resulting conformational changes inactivate the enzyme, making it unable to process substrate. | ||
== Caspase-7 Dynamics == | == Caspase-7 Dynamics == | ||
Observed here is the <scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7. These dynamics show the dramatic conformational change of the cleaved semi-ordered protease upon binding to the substrate mimic DEVD-CHO. Substrate binding triggers rearrangement of the partially ordered loop bundles and the L2' loop. The newly assumed state stabilizes the protein. | Observed here is the <scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7. These dynamics show the dramatic conformational change of the cleaved semi-ordered protease upon binding to the substrate mimic DEVD-CHO. Substrate binding triggers rearrangement of the partially ordered loop bundles and the L2' loop. The newly assumed state stabilizes the protein. | ||
== Notes == | == Notes == | ||