Structure of Bax: coregulation of dimer formation and intracellular localization
| Autor: | M, Suzuki, R J, Youle, N, Tjandra |
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| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Sequence Homology Amino Acid Recombinant Fusion Proteins Detergents Molecular Sequence Data bcl-X Protein Apoptosis Hydrogen-Ion Concentration Cell Compartmentation Protein Structure Tertiary Glucosides Proto-Oncogene Proteins c-bcl-2 Proto-Oncogene Proteins COS Cells Animals Humans Amino Acid Sequence Protein Structure Quaternary Dimerization Nuclear Magnetic Resonance Biomolecular bcl-2-Associated X Protein |
| Zdroj: | Cell. 103(4) |
| ISSN: | 0092-8674 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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