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={Bing Xiao and Richard J. Heath and Peter Saiu and Fiona C. Leiper and Philippe Leone and Chun Jing and Philip A Walker and Lesley F. Haire and John F. Eccleston and Colin T. Davis and Stephen R. Martin and David Carling and Steven J. Gamblin},
  journal={Nature},
  year={2007},
  volume={449},
  pages={496-500}
}
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… 
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