Abstract
Comparison between the BAD complexes indicated that BAD all docks a hydrophobic surface of PKAc regardless of its phosphorylation. PKAc may prevent Bcl-xL from rebinding to BAD by phosphorylating human BAD at Ser118; whereas human BAD is phosphorylated on Ser75 in a BAD-Bcl-xL complex, resulting in the dissociation of BAD.
Keywords: Computational modeling, protein-protein interaction, sequence alignment
Protein & Peptide Letters
Title: Molecular Modeling of Human BAD, a Pro-Apoptotic Bcl-2 Family Member, Integrating Glycolysis and Apoptosis
Volume: 17 Issue: 2
Author(s): Jie Yang
Affiliation:
Keywords: Computational modeling, protein-protein interaction, sequence alignment
Abstract: Comparison between the BAD complexes indicated that BAD all docks a hydrophobic surface of PKAc regardless of its phosphorylation. PKAc may prevent Bcl-xL from rebinding to BAD by phosphorylating human BAD at Ser118; whereas human BAD is phosphorylated on Ser75 in a BAD-Bcl-xL complex, resulting in the dissociation of BAD.
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Cite this article as:
Yang Jie, Molecular Modeling of Human BAD, a Pro-Apoptotic Bcl-2 Family Member, Integrating Glycolysis and Apoptosis, Protein & Peptide Letters 2010; 17 (2) . https://dx.doi.org/10.2174/092986610790226003
DOI https://dx.doi.org/10.2174/092986610790226003 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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