ArticlePloS one2014
Design rules for selective binding of nuclear localization signals to minor site of importin α.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Alternative bipartite arrangements of VP1 BR1-3 drive efficient nuclear import of AAV2 capsids.The Journal of biological chemistry · 2026Article
- The importin-alpha superfamily engages in ethylene signaling by shuttling ETHYLENE INSENSITIVE 2 from the endoplasmic reticulum to the nucleus.The FEBS journal · 2026Article
- Competitive Binding of Viral Nuclear Localization Signal Peptide and Inhibitor Ligands to Importin-α Nuclear Transport Protein.Journal of chemical information and modeling · 2024Article
- Binding of viral nuclear localization signal peptides to importin-α nuclear transport protein.Biophysical journal · 2023Article
- Article
- Review
- Variations in nuclear localization strategies among pol X family enzymes.Traffic (Copenhagen, Denmark) · 2018Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Structural analysis of the complex between influenza B nucleoprotein and human importin-α.Scientific reports · 2017Article
- DNA polymerase β contains a functional nuclear localization signal at its N-terminus.Nucleic acids research · 2017Article
- Conservation of inner nuclear membrane targeting sequences in mammalian Pom121 and yeast Heh2 membrane proteins.Molecular biology of the cell · 2015Article
- Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7.Structure (London, England : 1993) · 2015Article
- Calpain 5 is highly expressed in the central nervous system (CNS), carries dual nuclear localization signals, and is associated with nuclear promyelocytic leukemia protein bodies.The Journal of biological chemistry · 2014Article
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2 authors.
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Abstract
Selectivity is a critical issue in molecular recognition. However, design rules that underlie selectivity are often not well understood. Here, we studied five classical nuclear localization signals (NLSs) that contain the motif KRx(W/F/Y)xxAF and selectively bind to the minor site of importin α. The selectivity for the minor site is dissected by building structural models for the NLS-importin α complexes and analyzing the positive design and negative design in the NLSs. In our models, the KR residues of the motif occupy the P1' and P2' pockets of importin α, respectively, forming hydrogen-bonding and cation-π interactions. The aromatic residue at the P4' position plays dual roles in the selectivity for the minor site: by forming π-stacking with W357 of importin α to reinforce the minor-site binding; and by clashing with the P5 pocket in the major binding site. The F residue at the P8' position occupies a deep pocket, providing additional stabilization. The P7' position sits on a saddle next to the P8' pocket and hence requires a small residue; the A residue fulfills this requirement. The principal ideas behind these blind predictions turn out to be correct in an evaluation against subsequently available X-ray structures for the NLS-importin α complexes, but some details are incorrect. These results illustrate that the selectivity for the minor site can be achieved via a variety of design rules.
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