AMP-activated protein kinase undergoes nucleotide-dependent conformational changes

@article{Chen2012AMPactivatedPK,
  title={AMP-activated protein kinase undergoes nucleotide-dependent conformational changes},
  author={Lei Chen and Jue Wang and Yuan-Yuan Zhang and S Frank Yan and Dietbert Neumann and Uwe Schlattner and Zhi-Xin Wang and Jia-wei Wu},
  journal={Nature Structural \&Molecular Biology},
  year={2012},
  volume={19},
  pages={716-718}
}
The energy sensor AMP-activated protein kinase (AMPK) is a heterotrimeric complex that is allosterically activated by AMP binding to the γ subunit. Cocrystal structures of the mammalian AMPK core reveal occlusion of nucleotide-binding site 3 of the γ subunit in the presence of ATP. However, site 3 is occupied in the presence of AMP. Mutagenesis studies indicate that sites 3 and 4 are important for AMPK allosteric activation. 
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