The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP.

@article{Zhu2015TheMO,
  title={The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP.},
  author={Chun Feng Zhu and Wei Wei and Xin Peng and Yu Dong and Yong Xi Gong and Xiao Fang Yu},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2015},
  volume={71 Pt 3},
  pages={516-24}
}
SAMHD1 is the only known eukaryotic deoxynucleoside triphosphate triphosphohydrolase (dNTPase) and is a major regulator of intracellular dNTP pools. It has been reported to be a potent inhibitor of retroviruses such as HIV-1 and endogenous retrotransposons. Previous crystal structures have revealed that SAMHD1 is activated by dGTP-dependent tetramer formation. However, recent data have indicated that the primary activator of SAMHD1 is GTP, not dGTP. Therefore, how its dNTPase activity is… CONTINUE READING