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 cargoes for transport through the nuclear pore complex.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Acrylates / chemistry
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Acrylates / pharmacology
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Active Transport, Cell Nucleus / drug effects*
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Amino Acid Substitution
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Crystallography, X-Ray
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Exportin 1 Protein
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Fatty Acids, Unsaturated / chemistry
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Fatty Acids, Unsaturated / metabolism
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Fatty Acids, Unsaturated / pharmacology
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Humans
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Hydrolysis
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Karyopherins / antagonists & inhibitors
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Karyopherins / chemistry
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Karyopherins / genetics
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Karyopherins / metabolism*
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Models, Anatomic
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Mutagenesis, Site-Directed
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Nuclear Export Signals / genetics
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Protein Conformation
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Receptors, Cytoplasmic and Nuclear / antagonists & inhibitors
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Receptors, Cytoplasmic and Nuclear / chemistry
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Receptors, Cytoplasmic and Nuclear / genetics
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Receptors, Cytoplasmic and Nuclear / metabolism*
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Static Electricity
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Triazoles / chemistry
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Triazoles / pharmacology
Substances
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Acrylates
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Fatty Acids, Unsaturated
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KPT-185
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Karyopherins
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Nuclear Export Signals
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Receptors, Cytoplasmic and Nuclear
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Saccharomyces cerevisiae Proteins
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Triazoles
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leptomycin B
Associated data
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PDB/4HAT
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PDB/4HAU
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PDB/4HAV
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PDB/4HAW
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PDB/4HAX
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PDB/4HAY
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PDB/4HAZ
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PDB/4HB0
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PDB/4HB2
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PDB/4HB3
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PDB/4HB4