1f16
From Proteopedia
(New page: 200px<br /> <applet load="1f16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f16" /> '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTE...) |
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| - | [[Image:1f16.gif|left|200px]]<br /> | + | [[Image:1f16.gif|left|200px]]<br /><applet load="1f16" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1f16" /> | caption="1f16" /> | ||
'''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX'''<br /> | '''SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Apoptosis is stimulated by the insertion of Bax from the cytosol into | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1F16 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Suzuki, M.]] | [[Category: Suzuki, M.]] | ||
[[Category: Tjandra, N.]] | [[Category: Tjandra, N.]] | ||
| - | [[Category: Youle, R | + | [[Category: Youle, R J.]] |
[[Category: helical protein]] | [[Category: helical protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:41 2008'' |
Revision as of 10:33, 21 February 2008
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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 Feb 21 12:33:41 2008
