Structural basis for AMP binding to mammalian AMP-activated protein kinase

@article{Xiao2007StructuralBF,
  title={Structural basis for AMP binding to mammalian AMP-activated protein kinase},
  author={B. Xiao and R. Heath and P. Saiu and F. C. Leiper and P. L{\'e}one and C. Jing and P. A. Walker and L. Haire and J. Eccleston and C. T. Davis and S. Martin and D. Carling and S. Gamblin},
  journal={Nature},
  year={2007},
  volume={449},
  pages={496-500}
}
  • B. Xiao, R. Heath, +10 authors S. Gamblin
  • Published 2007
  • Biology, Medicine
  • Nature
  • AMP-activated protein kinase (AMPK) regulates cellular metabolism in response to the availability of energy and is therefore a target for type II diabetes treatment. It senses changes in the ratio of AMP/ATP by binding both species in a competitive manner. Thus, increases in the concentration of AMP activate AMPK resulting in the phosphorylation and differential regulation of a series of downstream targets that control anabolic and catabolic pathways. We report here the crystal structure of the… CONTINUE READING
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