Molecular Modeling of Human BAD, a Pro-Apoptotic Bcl-2 Family Member, Integrating Glycolysis and Apoptosis
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.
Document Type: Research Article
Publication date: February 1, 2010
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.