ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase

Huihao Zhou, Litao Sun, Xiang-Lei Yang and Paul Schimmel ()
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Huihao Zhou: The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Litao Sun: The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Xiang-Lei Yang: The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA
Paul Schimmel: The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2013, vol. 494, issue 7435, 121-124

Abstract: The crystal structure of prolyl tRNA synthetase simultaneously bound to its substrate ATP and its inhibitor halofuginone, a derivative of a compound used to treat malaria, indicates that (through interactions with ATP) halofuginone occupies both the amino acid and tRNA binding sites on the synthetase, revealing a new model for developing synthetase inhibitors.

Date: 2013
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DOI: 10.1038/nature11774

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