A bifunctional allosteric site in the dimer interface of procaspase-3

The dimer interface of caspase-3 contains a bifunctional allosteric site in which the enzyme can be activated or inactivated, depending on the context of the protein. In the mature caspase-3, the binding of allosteric inhibitors to the interface results in an order-to-disorder transition in the acti...

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Veröffentlicht in:	Biophysical chemistry 2011-11, Vol.159 (1), p.100-109
Hauptverfasser:	Schipper, Joshua L., MacKenzie, Sarah H., Sharma, Anil, Clark, A. Clay
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric activator Allosteric Site Apoptosis Cancer therapy Caspase Caspase 3 - chemistry Caspase 3 - metabolism Drug design Enzyme Activation - drug effects Humans Models, Molecular Protein Binding Protein Multimerization Small Molecule Libraries - chemistry Small Molecule Libraries - pharmacology
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