Nature Communications (Mar 2016)

Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding

  • Christopher G. Langendorf,
  • Kevin R. W. Ngoei,
  • John W. Scott,
  • Naomi X. Y. Ling,
  • Sam M. A. Issa,
  • Michael A. Gorman,
  • Michael W. Parker,
  • Kei Sakamoto,
  • Jonathan S. Oakhill,
  • Bruce E. Kemp

DOI
https://doi.org/10.1038/ncomms10912
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 8

Abstract

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AMPK regulates the metabolism and so drugs that activate AMPK might have potential for the treatment of metabolic disease. Here, the authors report the structure of AMPK bound to an activating compound, revealing two binding sites and indicating that dual therapy might be a good drug strategy.