P42574

Caspase-3 is a crucial aspartate-specific cysteine protease within the ICE subfamily, characterized by its structure as an inactive proenzyme that undergoes proteolytic cleavage to form an active heterodimer composed of p17 and p11 subunits. This structural transformation is essential for its role in apoptosis, where the active enzyme systematically dismantles cellular components by cleaving key substrates like PARP, thereby ensuring orderly cell death. The precise arrangement of the p17 and p11 subunits within caspase-3′s structure is vital for enzymatic activity and interaction with other proteins in the apoptotic cascade, including the activation of caspase-6, -7, and -9. Understanding the structural integrity of caspase-3 is fundamental for elucidating function in maintaining cellular homeostasis, eliminating damaged or unnecessary cells, and regulating processes such as development, immune response, and cancer prevention. Caspase-3′s structural domains facilitate localization and interaction within the cytoplasm, making caspase-3 a key player in various physiological and pathological contexts.