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Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL

Abstract : The SOUL protein is known to induce apoptosis by provoking the mitochondrial permeability transition and a sequence homologous to the Bcl-2 homology 3 (BH3) domains has been recently identified in it thus making it a potential new member of the BH3-only protein family. Here we present NMR, SPR and crystallographic evidence that a peptide spanning SOUL residues 147 - 172 interacts with the anti-apoptotic protein Bcl-xL. We have crystallized SOUL alone and the complex of its BH3 domain peptide with Bcl-xL and solved their three-dimensional structures. The SOUL monomer is a single domain organized as a distorted beta barrel with eight anti-parallel strands and two alpha helices. The BH3 domain extends across 15 residues at the end of the second helix and 8 amino acids in the chain following it. There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.
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Submitted on : Saturday, August 13, 2011 - 2:57:15 AM
Last modification on : Saturday, August 13, 2011 - 2:57:15 AM
Long-term archiving on: : Sunday, December 4, 2016 - 10:38:47 PM

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Emmanuele Ambrosi, Stefano Capaldi, Michele Bovi, Gianmaria Saccomani, Massimiliano Perduca, et al.. Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Biochemical Journal, Portland Press, 2011, 438 (2), pp.291-301. ⟨10.1042/BJ20110257⟩. ⟨hal-00614614⟩

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