Evolution of the conformational ensemble and allosteric networks of apoptotic caspases in chordates.

ABSTRACT: Apoptotic caspases exist not as static structures but as dynamic ensembles in solution, finely tuned by post-translational modifications and oligomerization. The fine-tuning of this ensemble by cellular cues allows caspases to influence not only apoptotic pathways but also the non-apoptotic pathways in which they are involved. These ensembles span a complex conformational landscape from well-characterized low-energy states captured in structural databases to transient high-energy intermediates that remain elusive and poorly understood. This limited structural view poses a major barrier to fully understanding how caspase activity is regulated and diversified across cellular contexts. To address this, we integrate evolutionary, folding, and mutational data with molecular dynamics simulations

SUBMITTER: Joglekar I 

PROVIDER: S-EPMC12409990 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature