Molecular modeling of human BAD, a pro-apoptotic Bcl-2 family member, integrating glycolysis and apoptosis.
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.
Yang
J
J
State Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry and Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, P.R.China. luckyjyj@sina.com
D048948:14-3-3 Proteins / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D017209:Apoptosis; D051023:BH3 Interacting Domain Death Agonist Protein / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D019295:Computational Biology / Q000379:methods; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D030562:Databases, Protein; D006019:Glycolysis; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D054645:Protein Phosphatase 1 / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D013499:Surface Properties; D051025:bcl-Associated Death Protein / Q000737:chemistry* / Q000378:metabolism; D051020:bcl-X Protein / Q000737:chemistry* / Q000378:metabolism
D048948:14-3-3 Proteins; D000596:Amino Acids; C494819:BAD protein, human; D051023:BH3 Interacting Domain Death Agonist Protein; D051025:bcl-Associated Death Protein; D051020:bcl-X Protein; D017868:Cyclic AMP-Dependent Protein Kinases; D054645:Protein Phosphatase 1