Fig. 2: Simulations of protein aggregation. | Experimental & Molecular Medicine

Fig. 2: Simulations of protein aggregation.

From: Optogenetic engineering of BAX to control mitochondrial permeabilization and attenuate apoptosis in cells

Fig. 2: Simulations of protein aggregation.

a A schematic representation of rBAX, endo-BAX and rTOMM20 interactions. Under dark conditions, the three components remain dissociated. Upon blue light exposure, however, they assemble at the MOM. In this system, rBAX and rTOMM20 interact via CRY2–CIB1 binding, whereas rBAX and endo-BAX associate through their BH grooves. b To model optogenetically induced BAX aggregation, AlphaFold Multimer simulations were performed using either HBAXS184E or DBAXS184E at a 6:4 ratio to endo-BAX (total of ten proteins). Each protein is rendered in a different color, with BH grooves, α9 helices, endo-BAX or rBAX highlighted in green. In contrast to endo-BAX and HBAXS184E, the DBAXS184E complex exhibits minimal pore formation. c To simulate conditions in which rTOMM20 associates with rBAX under blue light irradiation, endo-BAX, rBAX and rTOMM20 were combined in a 5:3:2 ratio. Membrane-embedded residues are highlighted in pink, and the remnants are shown in gray. Both the top and side views are presented. The DBAXS184E–rTOMM20 (DBT) complex displays limited hydrophobic motif insertion into the MOM compared to the HBAXS184E–rTOMM20 (HBT) complex.

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