1zy3: Difference between revisions

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New page: left|200px<br /> <applet load="1zy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zy3" /> '''Structural model of complex of Bcl-w protei...
 
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[[Image:1zy3.gif|left|200px]]<br />
[[Image:1zy3.gif|left|200px]]<br /><applet load="1zy3" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1zy3" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1zy3" />
caption="1zy3" />
'''Structural model of complex of Bcl-w protein with Bid BH3-peptide'''<br />
'''Structural model of complex of Bcl-w protein with Bid BH3-peptide'''<br />


==Overview==
==Overview==
A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This, binding induced major conformational rearrangements in both the peptide, and protein components of the complex and led to the displacement and, unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with, a bound BID-BH3 peptide was determined using NMR spectroscopy and, molecular docking. These studies confirmed that a region of 16 residues of, the BID-BH3 peptide is responsible for its strong binding to BCL-w and, BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with, dodecylphosphocholine micelles were characterized and showed that the, conformational change of BCL-w upon lipid binding occurred at the same, time as the release and unfolding of the BH3 peptide.
A peptide corresponding to the BH3 region of the proapoptotic protein, BID, could be bound in the cleft of the antiapoptotic protein, BCL-w. This binding induced major conformational rearrangements in both the peptide and protein components of the complex and led to the displacement and unfolding of the BCL-w C-terminal alpha-helix. The structure of BCL-w with a bound BID-BH3 peptide was determined using NMR spectroscopy and molecular docking. These studies confirmed that a region of 16 residues of the BID-BH3 peptide is responsible for its strong binding to BCL-w and BCL-x(L). The interactions of BCL-w and the BID-BH3 peptide complex with dodecylphosphocholine micelles were characterized and showed that the conformational change of BCL-w upon lipid binding occurred at the same time as the release and unfolding of the BH3 peptide.


==About this Structure==
==About this Structure==
1ZY3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1ZY3 OCA].  
1ZY3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1ZY3 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Denisov, A.Y.]]
[[Category: Denisov, A Y.]]
[[Category: Gehring, K.]]
[[Category: Gehring, K.]]
[[Category: apoptosis]]
[[Category: apoptosis]]
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[[Category: bh3-peptide]]
[[Category: bh3-peptide]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:43:01 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:12 2008''