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1f16
From Proteopedia
| 1f16, 20 NMR models () | |||||||||
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| Domains: | Bcl-2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
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.
Structure of Bax: coregulation of dimer formation and intracellular localization., Suzuki M, Youle RJ, Tjandra N, Cell. 2000 Nov 10;103(4):645-54. PMID:11106734
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1F16 is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Suzuki M, Youle RJ, Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell. 2000 Nov 10;103(4):645-54. PMID:11106734
Page seeded by OCA on Tue Feb 17 13:30:11 2009
