期刊
JOURNAL OF MOLECULAR GRAPHICS & MODELLING
卷 67, 期 -, 页码 94-101出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jmgm.2016.05.007
关键词
BAX; BIM SAHB; Molecular dynamics simulation; Apoptosis
类别
资金
- Council of Scientific and Industrial Research (CSIR), India
The interaction of BAX (BCL-2-associated X protein) with BIM (BCL-2 interacting mediator of cell death) SAHB (stabilized alpha helix of BCL2) directly initiates BAX-mediated mitochondrial apoptosis. This molecular dynamics study reveals that BIM SAHB forms a stable complex with BAX but it remains in a non-functional conformation. N terminal of BAX folds towards the core which has been reported exposed in the functional monomer. The alpha 1-alpha 2 loop, which has been reported in open conformation in functional BAX, acquires a closed conformation during the simulation. BH3/alpha 2 remains less exposed as compared to initial structure. The hydrophobic residues of BIM accommodates in the rear pocket of BAX during the simulation. A steep decrease in radius of gyration and solvent accessible surface area (SASA) indicates the complex folding to acquire a more stable but inactive conformation. Further the covariance matrix reveals that the backbone atoms' motions favour the inactive conformation of the complex. This is the first report on the non-functional BAX-BIM SAHB complex by molecular dynamics simulation in the best of our knowledge. (C) 2016 Elsevier Inc. All rights reserved.
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