Molecular Playground/Executioner Caspase-7: Difference between revisions
New page: Caspases are a family of CBI Molecules being studied in the [http://www.chem.umass.edu/~jhardy/ Hardy Lab] in the <span class="plainlinks">[http://www.umass.edu/cbi/ University of Mas... |
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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 == | |||
This is an updated version of the [http://www.proteopedia.org/wiki/index.php/Molecular_Playground/Caspase-7_Dynamics Caspase-7 Dynamics] page. | |||
== References == | == References == | ||