Skip to main content
. 2012 Jun 14;8(6):e1002565. doi: 10.1371/journal.pcbi.1002565

Figure 1. Bax undergoes several conformational changes enabling it to form pores in the mitochondrial outer membrane.

Figure 1

(A) Bax activation leads to mitochondrial outer membrane permeabilization (MOMP). Inactive Bax is a cytosolic monomer. Activator-induced opening of loop 1–2 allows the activator to bind. Subsequently, the C-domain of the now active Bax vacates the BH groove and inserts into the mitochondrial membrane. Additionally, the Bax BH3 domain gets exposed. Bax oligomerization ensues via the BH groove and the BH3 domain, eventually leading to the formation of pores which permeabilize the membrane. (B) Location of the BH3 domain (cyan), the C-domain (yellow), loop 1–2 (pink) in inactive Bax (the rest of the protein in gray). (C) Location of above domains (same color coding) in active Bax (the rest of the protein in orange). The activator peptide Bim-SAHB is shown in purple.