Maureen E. Hill/Sandbox1

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== Forms of Caspase-7 ==
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== Caspase-7 Dynamics ==
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<scene name='Molecular_Playground/Caspase_Dynamics/1f1j/2'>Caspase-7 bound to suicide inhibitor/substrate mimic DEVD-CHO</scene>, trapping protein in active/substrate bound conformation.
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<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7. Upon substrate binding, the loop bundle rearranges and stabilizes the protein.
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<scene name='Molecular_Playground/Caspase_Dynamics/1shj-234234/1'>Caspase-7 bound to allosteric inhibitor DICA through CYS290</scene> trapping protein in a form incompatible with substrate binding.
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<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.
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Revision as of 18:21, 3 December 2013

Caspases are a family of CBI Molecules being studied in the Hardy Lab in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

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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