Structure-based design of a pathway-specific nuclear import inhibitor
AE Cansizoglu, BJ Lee, ZC Zhang… - Nature structural & …, 2007 - nature.com
AE Cansizoglu, BJ Lee, ZC Zhang, BMA Fontoura, YM Chook
Nature structural & molecular biology, 2007•nature.comKapβ2 (also called transportin) recognizes PY nuclear localization signal (NLS), a new class
of NLS with a R/H/Kx (2–5) PY motif. Here we show that Kapβ2 complexes containing
hydrophobic and basic PY-NLSs, as classified by the composition of an additional N-
terminal motif, converge in structure only at consensus motifs, which explains ligand
diversity. On the basis of these data and complementary biochemical analyses, we designed
a Kapβ2-specific nuclear import inhibitor, M9M.
of NLS with a R/H/Kx (2–5) PY motif. Here we show that Kapβ2 complexes containing
hydrophobic and basic PY-NLSs, as classified by the composition of an additional N-
terminal motif, converge in structure only at consensus motifs, which explains ligand
diversity. On the basis of these data and complementary biochemical analyses, we designed
a Kapβ2-specific nuclear import inhibitor, M9M.
Abstract
Kapβ2 (also called transportin) recognizes PY nuclear localization signal (NLS), a new class of NLS with a R/H/Kx(2–5)PY motif. Here we show that Kapβ2 complexes containing hydrophobic and basic PY-NLSs, as classified by the composition of an additional N-terminal motif, converge in structure only at consensus motifs, which explains ligand diversity. On the basis of these data and complementary biochemical analyses, we designed a Kapβ2-specific nuclear import inhibitor, M9M.
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