1zy3

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(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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<applet load="1zy3" size="450" color="white" frame="true" align="right" spinBox="true"
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'''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==
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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.
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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==
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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].
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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]]
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[[Category: Denisov, A.Y.]]
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[[Category: Denisov, A Y.]]
[[Category: Gehring, K.]]
[[Category: Gehring, K.]]
[[Category: apoptosis]]
[[Category: apoptosis]]
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[[Category: bh3-peptide]]
[[Category: bh3-peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:43:01 2007''
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''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


1zy3

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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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