Crystal structures of human SIRT3 displaying substrate-induced conformational changes.

@article{Jin2009CrystalSO,
  title={Crystal structures of human SIRT3 displaying substrate-induced conformational changes.},
  author={Lei Jin and Wentao Wei and Yaobin Jiang and Hao Peng and Jianhua Cai and Chen Mao and Han Dai and Wendy Choy and Jean E. Bemis and Michael R. Jirousek and Jill C. Milne and Christoph Westphal and Robert B. Perni},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 36},
  pages={24394-405}
}
SIRT3 is a major mitochondrial NAD(+)-dependent protein deacetylase playing important roles in regulating mitochondrial metabolism and energy production and has been linked to the beneficial effects of exercise and caloric restriction. SIRT3 is emerging as a potential therapeutic target to treat metabolic and neurological diseases. We report the first sets of crystal structures of human SIRT3, an apo-structure with no substrate, a structure with a peptide containing acetyl lysine of its natural… CONTINUE READING
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