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.


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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • COS Cells
  • Cell Compartmentation
  • Detergents / pharmacology
  • Dimerization
  • Glucosides / pharmacology
  • Humans
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins / drug effects
  • Proto-Oncogene Proteins / isolation & purification
  • Proto-Oncogene Proteins c-bcl-2 / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Sequence Homology, Amino Acid
  • bcl-2-Associated X Protein
  • bcl-X Protein


  • BAX protein, human
  • BCL2L1 protein, human
  • Detergents
  • Glucosides
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Fusion Proteins
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • octyl-beta-D-glucoside

Associated data

  • PDB/1F16