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

Article Details

Citation

Ambrosi E, Capaldi S, Bovi M, Saccomani G, Perduca M, Monaco HL

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

Biochem J. 2011 Sep 1;438(2):291-301. doi: 10.1042/BJ20110257.

PubMed ID
21639858 [ View in PubMed
]
Abstract

The SOUL protein is known to induce apoptosis by provoking the mitochondrial permeability transition, and a sequence homologous with the BH3 (Bcl-2 homology 3) domains has recently been identified in the protein, thus making it a potential new member of the BH3-only protein family. In the present study, we provide NMR, SPR (surface plasmon resonance) and crystallographic evidence that a peptide spanning residues 147-172 in SOUL 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 eight 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Bcl-2-like protein 1Q07817Details