Structure-based design of a pathway-specific nuclear import inhibitor
- 15 April 2007
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 14 (5) , 452-454
- https://doi.org/10.1038/nsmb1229
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.Keywords
This publication has 15 references indexed in Scilit:
- Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2Cell, 2006
- Two motifs essential for nuclear import of the hnRNP A1 nucleocytoplasmic shuttling sequence M9 coreFEBS Letters, 2006
- Karyopherins: from nuclear-transport mediators to nuclear-function regulatorsTrends in Cell Biology, 2004
- Nuclear import and activity of histone deacetylase in Xenopus oocytes is regulated by phosphorylationJournal of Cell Science, 2004
- Transportin2 functions as importin and mediates nuclear import of HuRProceedings of the National Academy of Sciences, 2004
- Uncoupling Kapβ2 Substrate Dissociation and Ran BindingBiochemistry, 2002
- The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mappingNucleic Acids Research, 1996
- The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteinsNucleic Acids Research, 1993
- Nuclear targeting sequences — a consensus?Trends in Biochemical Sciences, 1991
- Leptomycins A and B, new antifungal antibiotics. I. Taxonomy of the producing strain and their fermentation, purification and characterization.The Journal of Antibiotics, 1983