The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural Basis for the Specificity of Bipartite Nuclear Localization Sequence Binding by Importin-α
Open accessAbstract
Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins.
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Cites
A motif-based profile scanning approach for genome-wide prediction of signaling pathways
Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., & Cantley, L. C. (2001) · Nature Biotechnology · doi:10.1038/86737 · Cited by 517
Fontes, M. R. M., Teh, T., & Kobe, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3642 · Cited by 398
Self-citation
Cited by
Importin α: a multipurpose nuclear-transport receptor
Goldfarb, D. S., Corbett, A. H., Mason, D. A., Harreman, M. T., & Adam, S. A. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.07.016 · Cited by 658
Six Classes of Nuclear Localization Signals Specific to Different Binding Grooves of Importin α
Kosugi, S., Hasebe, M., Matsumura, N., Takashima, H., Miyamoto-Sato, E., Tomita, M., & Yanagawa, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807017200 · Cited by 615
The broad spectrum antiviral ivermectin targets the host nuclear transport importin α/β1 heterodimer
Yang, S. N. Y., Atkinson, S. C., Wang, C., Lee, A., Bogoyevitch, M. A., Borg, N. A., & Jans, D. A. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104760 · Cited by 322
Self-citationStructural basis for activation of fungal sterol receptor Upc2 and azole resistance
Tan, L., Chen, L., Yang, H., Jin, B., Kim, G., & Im, Y. J. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01117-0 · Cited by 38
Metadata
- Authors
- Fontes, M. R. M., Teh, T., Jans, D., Brinkworth, R. I., & Kobe, B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 278
- Issue
- 30
- Pages
- 27981-27987
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1995160911
- Cited by
- 186
- References
- 2
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Fontes, M. R. M., Teh, T., Jans, D., Brinkworth, R. I., & Kobe, B. (2003). Structural Basis for the Specificity of Bipartite Nuclear Localization Sequence Binding by Importin-α. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m303275200
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