1f16: Difference between revisions
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'''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX''' | '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX''' | ||
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[[Category: Tjandra, N.]] | [[Category: Tjandra, N.]] | ||
[[Category: Youle, R J.]] | [[Category: Youle, R J.]] | ||
[[Category: | [[Category: Helical protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:46:12 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:46, 2 May 2008
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| 1f16, 20 NMR models (default scene) | |||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
Overview
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.
About this Structure
1F16 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 15:46:12 2008
