Structure of Bax: coregulation of dimer formation and intracellular localization.
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Suzuki M, Youle RJ, Tjandra N
Structure of Bax: coregulation of dimer formation and intracellular localization.
Cell. 2000 Nov 10;103(4):645-54. doi: 10.1016/s0092-8674(00)00167-7.
- PubMed ID
- 11106734 [ View in PubMed]
- Abstract
Apoptosis is stimulated by the insertion of Bax from the cytosol into mitochondrial membranes. The solution structure of Bax, including the putative transmembrane domain at the C terminus, was determined in order to understand the regulation of its subcellular location. Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor, Bcl-x(L). The C-terminal alpha 9 helix occupies the hydrophobic pocket proposed previously to mediate heterodimer formation and bioactivity of opposing members of the Bcl-2 family. The Bax structure shows that the orientation of helix alpha 9 provides simultaneous control over its mitochondrial targeting and dimer formation.