This week in techniques

Approach

Summary

Licensing status

Publication and contact information

Drug platforms

Crystal structure of the antifibrotic halofuginone bound to the prolyl-tRNA synthetase domain of human glutamyl-prolyl-tRNA synthetase (EPRS)

The crystal structure of the antifibrotic halofuginone bound to the prolyl-tRNA synthetase domain of human EPRS could aid the development of new compounds to target the synthetase. Halofuginone is a halogenated derivative of the alkaloid febrifugine, which is the active compound in a Chinese herb used to treat malaria-induced fever. The crystal structure showed that halofuginone is an ATP-dependent inhibitor. Next steps could include optimizing the halofuginone analogs and determining how such compounds bind to other tRNA synthetases.

SciBX 6(3); doi:10.1038/scibx.2013.73
Published online Jan. 24, 2013

Unpatented; aTyr Pharma Inc. has an exclusive option to license the work

Zhou, H. et al. Nature; published online Dec. 23, 2012;
doi:10.1038/nature11774
Contact: Paul Schimmel, The Scripps Research Institute, La Jolla, Calif.
e-mail:

schimmel@scripps.edu