Crystal structures of Aedes aegypti kynurenine aminotransferase

  title={Crystal structures of Aedes aegypti kynurenine aminotransferase},
  author={Q. Han and Y. Gao and H. Robinson and Haizhen Ding and S. Wilson and J. Li},
  journal={The FEBS Journal},
  • Q. Han, Y. Gao, +3 authors J. Li
  • Published 2005
  • Biology, Medicine
  • The FEBS Journal
  • Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7‐nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 Å, respectively. The structure was solved by a combination of single‐wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with… CONTINUE READING
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