Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site.

@article{Liu2011CrystalSO,
  title={Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site.},
  author={Qiang Liu and Yunfeng Shen and Sanling Liu and Jianping Weng and Jinsong Liu},
  journal={FEBS letters},
  year={2011},
  volume={585 8},
  pages={1175-9}
}
Human glucokinase (GK) plays an important role in glucose homeostasis. An E339K mutation in GK was recently found to be associated with hyperglycemia. It showed lower enzyme activity and impaired protein stability compared to the wild-type enzyme. Here, we present the crystal structure of E339K GK in complex with glucose. This mutation results in a conformational change of His416, spatially interfering with adenosine-triphosphate (ATP) binding. Furthermore, Ser411 at the ATP binding site is… CONTINUE READING

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