1f16
From Proteopedia
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| - | [[Image:1f16.gif|left|200px]] | + | [[Image:1f16.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX''' | + | {{Structure |
| + | |PDB= 1f16 |SIZE=350|CAPTION= <scene name='initialview01'>1f16</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F16 is a [ | + | 1F16 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F16 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11106734 11106734] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helical protein]] | [[Category: helical protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:03 2008'' |
Revision as of 09:03, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
Contents |
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.
Disease
Known diseases associated with this structure: Colorectal cancer OMIM:[600040], T-cell acute lymphoblastic leukemia OMIM:[600040]
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 Thu Mar 20 11:03:03 2008
