AI Article Synopsis
- A peptide from the proapoptotic protein BID binds to the antiapoptotic protein BCL-w, causing significant changes in both proteins' structures.
- The binding results in the unfolding of a specific part of BCL-w, particularly its C-terminal alpha-helix, which is crucial for its function.
- Research using NMR spectroscopy and molecular docking reveals that a 16-residue segment of the BID-BH3 peptide is key to its strong interaction with BCL-w and BCL-x(L), and this interaction is influenced by lipid binding.
Article Abstract
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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| http://dx.doi.org/10.1021/bi052332s | DOI Listing |
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