ArticleBiophysical chemistry2011
A bifunctional allosteric site in the dimer interface of procaspase-3.
Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- The impact of cycleanine in cancer research: a computational study.Journal of molecular modeling · 2022Article
- Cassaine Diterpenoid Amide from Stem Bark ofMolecules (Basel, Switzerland) · 2020Article
- New Alkoxy Flavone Derivatives Targeting Caspases: Synthesis and Antitumor Activity Evaluation.Molecules (Basel, Switzerland) · 2018Article
- Derivatives of Procaspase-Activating Compound 1 (PAC-1) and their Anticancer Activities.Current medicinal chemistry · 2016Article
- Removal of Metabolic Liabilities Enables Development of Derivatives of Procaspase-Activating Compound 1 (PAC-1) with Improved Pharmacokinetics.Journal of medicinal chemistry · 2015Article
- Specificity of a protein-protein interface: local dynamics direct substrate recognition of effector caspases.Proteins · 2014Article
- Turning on caspases with genetics and small molecules.Methods in enzymology · 2014Review
- Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.The Journal of biological chemistry · 2012Article
- Allosteric modulation of caspase 3 through mutagenesis.Bioscience reports · 2012Article
- Death by caspase dimerization.Advances in experimental medicine and biology · 2012Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
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 active site loops. In procaspase-3, by contrast, the binding of allosteric activators to the interface results in a disorder-to-order transition in the active site. We have utilized the allosteric site to identify a small molecule activator of procaspase and to characterize its binding to the protease. The data suggest that an efficient activator must stabilize the active conformer of the zymogen by expelling the intersubunit linker from the interface, and it must interact with active site residues found in the allosteric site. Small molecule activators that fulfill the two requirements should provide scaffolds for drug candidates as a therapeutic strategy for directly promoting procaspase-3 activation in cancer cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.