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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Revision as of 18:36, 12 November 2007
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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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