The binding of β-d-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: A new class of inhibitors.

@article{Alexacou2010TheBO,
  title={The binding of $\beta$-d-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: A new class of inhibitors.},
  author={K.-M. Alexacou and Alia-Cristina Tenchiu Deleanu and Evangelia D Chrysina and Maria-Despoina Charavgi and Ioannis D. Kostas and Spyros E Zographos and Nikos G. Oikonomakos and Demetres D. Leonidas},
  journal={Bioorganic \& medicinal chemistry},
  year={2010},
  volume={18 22},
  pages={
          7911-22
        }
}

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The structure of muscle glycogen phosphorylase b (GPb) complexed with the two compounds at 2.0 A and 1.8 A resolution reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change in the tertiary structure.
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A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity.
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