Conformational flexibility in the allosteric regulation of human UDP-α-D-glucose 6-dehydrogenase.

@article{Sennett2011ConformationalFI,
  title={Conformational flexibility in the allosteric regulation of human UDP-α-D-glucose 6-dehydrogenase.},
  author={Nicholas C Sennett and Renuka Kadirvelraj and Zachary A Wood},
  journal={Biochemistry},
  year={2011},
  volume={50 44},
  pages={9651-63}
}
UDP-α-D-xylose (UDX) acts as a feedback inhibitor of human UDP-α-D-glucose 6-dehydrogenase (hUGDH) by activating an unusual allosteric switch, the Thr131 loop. UDX binding induces the Thr131 loop to translate ~5 Å through the protein core, changing packing interactions and rotating a helix (α6(136-144)) to favor the formation of an inactive hexameric complex. But how does to conformational change occur given the steric packing constraints of the protein core? To answer this question, we deleted… CONTINUE READING

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