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Qingxiang Sun; Yazmin P. Carrasco; Youcai Hu; Xiaofeng Guo; Hamid Mirzaei; John MacMillan; Yuh Min Chook(Profiled Authors: Yuh Min Chook; Xiaofeng Guo; John B MacMillan; Hamid Mirzaei)
Proceedings of the National Academy of Sciences of the United States of America. 2013;110(4):1303-1308.Abstract
The polyketide natural product Leptomycin B inhibits nuclear export mediated by the karyopherin protein chromosomal region maintenance 1 (CRM1). Here, we present 1.8- to 2.0-Å-resolution crystal structures of CRM1 bound to Leptomycin B and related inhibitors Anguinomycin A and Ratjadone A. Structural and complementary chemical analyses reveal an unexpected mechanism of inhibition involving covalent conjugation and CRM1-mediated hydrolysis of the natural products' lactone rings. Furthermore, mutagenesis reveals the mechanism of hydrolysis by CRM1. The nuclear export signal (NES)-binding groove of CRM1 is able to drive a chemical reaction in addition to binding protein cargos for transport through the nuclear pore complex.
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