1o0l: Difference between revisions

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New page: left|200px<br /> <applet load="1o0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o0l" /> '''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR T...
 
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[[Image:1o0l.gif|left|200px]]<br />
[[Image:1o0l.gif|left|200px]]<br /><applet load="1o0l" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1o0l" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1o0l" />
caption="1o0l" />
'''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY'''<br />
'''THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY'''<br />


==Overview==
==Overview==
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the, pro-apoptotic BH3-only proteins. The solution structure of the, pro-survival protein Bcl-w, presented here, reveals that the binding, groove is not freely accessible as predicted by previous structures of, pro-survival Bcl-2-like molecules. Unexpectedly, the groove appears to be, occluded by the C-terminal residues. Binding and kinetic data suggest that, the C-terminal residues of Bcl-w and Bcl-x(L) modulate pro-survival, activity by regulating ligand access to the groove. Binding of the, BH3-only proteins, critical for cell death initiation, is likely to, displace the hydrophobic C-terminal region of Bcl-w and Bcl-x(L)., Moreover, Bcl-w does not act only by sequestering the BH3-only proteins., There fore, pro-survival Bcl-2-like molecules probably control the, activation of downstream effectors by a mechanism that remains to be, elucidated.
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution structure of the pro-survival protein Bcl-w, presented here, reveals that the binding groove is not freely accessible as predicted by previous structures of pro-survival Bcl-2-like molecules. Unexpectedly, the groove appears to be occluded by the C-terminal residues. Binding and kinetic data suggest that the C-terminal residues of Bcl-w and Bcl-x(L) modulate pro-survival activity by regulating ligand access to the groove. Binding of the BH3-only proteins, critical for cell death initiation, is likely to displace the hydrophobic C-terminal region of Bcl-w and Bcl-x(L). Moreover, Bcl-w does not act only by sequestering the BH3-only proteins. There fore, pro-survival Bcl-2-like molecules probably control the activation of downstream effectors by a mechanism that remains to be elucidated.


==About this Structure==
==About this Structure==
1O0L 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=1O0L OCA].  
1O0L 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=1O0L OCA].  


==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Day, C.L.]]
[[Category: Day, C L.]]
[[Category: Harrison, P.J.]]
[[Category: Harrison, P J.]]
[[Category: Hinds, M.G.]]
[[Category: Hinds, M G.]]
[[Category: Huang, D.C.S.]]
[[Category: Huang, D C.S.]]
[[Category: Lackmann, M.]]
[[Category: Lackmann, M.]]
[[Category: Skea, G.L.]]
[[Category: Skea, G L.]]
[[Category: apoptosis]]
[[Category: apoptosis]]
[[Category: bcl-2]]
[[Category: bcl-2]]
Line 26: Line 25:
[[Category: helical bundle]]
[[Category: helical bundle]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:03 2008''