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1f16

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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.]]
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[[Category: Youle, R J.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:46:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:45 2008''
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Revision as of 12:46, 2 May 2008

Image:1f16.gif


PDB ID 1f16

Drag the structure with the mouse to rotate
1f16, 20 NMR models ()
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

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