1f16: Difference between revisions

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New page: left|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"  
<applet load="1f16" size="450" color="white" frame="true" align="right" spinBox="true"  
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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F16 OCA].  
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.J.]]
[[Category: Youle, R J.]]
[[Category: helical protein]]
[[Category: helical protein]]


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