1zy3
From Proteopedia
(New page: 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=" | + | |
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 | + | 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:// | + | 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 | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:12 2008'' |
Revision as of 14:20, 21 February 2008
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Structural model of complex of Bcl-w protein with Bid BH3-peptide
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.
About this Structure
1ZY3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles., Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K, Biochemistry. 2006 Feb 21;45(7):2250-6. PMID:16475813
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