Crystal structure, biochemical and cellular activities demonstrate separate functions of MTH1 and MTH2

@inproceedings{Carter2015CrystalSB,
  title={Crystal structure, biochemical and cellular activities demonstrate separate functions of MTH1 and MTH2},
  author={Megan H Carter and Ann-Sofie Jemth and Anna Hagenkort and Brent D. G. Page and Robert Gustafsson and Julia J Griese and Helge Gad and Nicholas C K Valerie and Matthieu Desroses and Johan Bostr{\"o}m and Ulrika Warpman Berglund and Thomas Helleday and P{\aa}l Stenmark},
  booktitle={Nature communications},
  year={2015}
}
Deregulated redox metabolism in cancer leads to oxidative damage to cellular components including deoxyribonucleoside triphosphates (dNTPs). Targeting dNTP pool sanitizing enzymes, such as MTH1, is a highly promising anticancer strategy. The MTH2 protein, known as NUDT15, is described as the second human homologue of bacterial MutT with 8-oxo-dGTPase activity. We present the first NUDT15 crystal structure and demonstrate that NUDT15 prefers other nucleotide substrates over 8-oxo-dGTP. Key… CONTINUE READING
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