1F16
SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
Summary for 1F16
| Entry DOI | 10.2210/pdb1f16/pdb |
| Descriptor | PROTEIN (APOPTOSIS REGULATOR BAX, MEMBRANE ISOFORM ALPHA) (1 entity in total) |
| Functional Keywords | helical protein, apoptosis |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform Alpha: Mitochondrion membrane; Single-pass membrane protein. Isoform Beta: Cytoplasm. Isoform Gamma: Cytoplasm. Isoform Delta: Cytoplasm (Potential): Q07812 |
| Total number of polymer chains | 1 |
| Total formula weight | 21204.35 |
| Authors | Suzuki, M.,Youle, R.J.,Tjandra, N. (deposition date: 2000-05-18, release date: 2000-11-22, Last modification date: 2024-05-22) |
| Primary citation | Suzuki, M.,Youle, R.J.,Tjandra, N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell(Cambridge,Mass.), 103:645-654, 2000 Cited by 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. PubMed: 11106734DOI: 10.1016/S0092-8674(00)00167-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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