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Structural and dynamic basis of indirect apoptosis inhibition by Bcl-xL: a case study with Bid

Elsner, C.; Hanke, A.; Vadas, O.; Gervasio, F. L.; Bordignon, E.

2025-09-04 biophysics
10.1101/2025.08.31.673340 bioRxiv
Show abstract

Intrinsic apoptosis is a form of cell death which is activated, executed and inhibited by the Bcl-2 protein family. The structural basis of the inhibition mechanisms remains elusive. Here, we characterize the ensemble structure of the inhibitory Bcl-xL/tBid complex at the mitochondrial membrane by probing inter-residue distances and dynamic solvent accessibilities complemented by integrative modelling and molecular dynamics simulations. We show that Bcl-xL and tBid form a heterodimer anchored to the membrane by the C-terminal helix of Bcl-xL. The BH3 domain of tBid is wedged between the exposed hydrophobic groove of Bcl-xL and the membrane headgroups, while tBids C-terminal helices remain dynamically engaged with the bilayer. This dynamic architecture sheds light on the mechanism of indirect inhibition of apoptosis.

Published in Proceedings of the National Academy of Sciences (predicted rank #1) · training set

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