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Related Concept Videos

Caspases01:24

Caspases

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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
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Caspase Allostery and Conformational Selection.

A Clay Clark1

  • 1Department of Biology, University of Texas at Arlington , Arlington, Texas 76019, United States.

Chemical Reviews
|January 12, 2016
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Summary
This summary is machine-generated.

Caspase proteases regulate apoptosis and inflammation. This review explores how cells control caspase activity through conformational changes and allosteric modulation, offering insights for therapeutic drug design.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Caspase proteases are key regulators of apoptosis and inflammation.
  • Detailed knowledge exists on caspase activation cascades.
  • Cellular mechanisms for fine-tuning caspase activity to prevent apoptosis remain unclear.

Purpose of the Study:

  • To provide a comprehensive overview of the caspase conformational landscape.
  • To elucidate mechanisms controlling caspase activity.
  • To highlight the role of allosteric modulation in fine-tuning caspase function.

Main Methods:

  • Review of existing literature and structural databases.
  • Analysis of caspase active and inactive conformations.
  • Examination of post-translational modifications and allosteric effectors.

Main Results:

  • Caspase activity is modulated by post-translational modifications and allosteric site binding.
  • Structural databases reveal diverse active and inactive caspase conformations.
  • Databases on caspase modifications are incomplete, limiting understanding of allosteric communication.

Conclusions:

  • Cells utilize a complex conformational landscape to control caspase activity.
  • Allosteric control offers opportunities for therapeutic intervention.
  • Further research is needed to fully understand allosteric modulation of caspases.