Crystallization and preliminary X-ray crystallographic analysis of importin-α from Neurospora crassa
| Autor: | Marcos R.M. Fontes, Maria Célia Bertolini, Natalia E. Bernardes, Agnes A.S. Takeda, Fernanda Zanolli Freitas |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
alpha Karyopherins
Biophysics Importin macromolecular substances Biology Crystallography X-Ray Biochemistry environment and public health Neurospora crassa Structural Biology Genetics Importin-alpha NLS Nuclear pore Nuclear protein Cell Nucleus fungi Condensed Matter Physics biology.organism_classification Recombinant Proteins Transport protein Crystallography Crystallization Communications health occupations Crystallization Oligopeptides Nuclear localization sequence Protein Binding |
| Zdroj: | Acta crystallographica. Section F, Structural biology communications. 70(Pt 4) |
| ISSN: | 2053-230X |
| Popis: | Importin-α recognizes cargo proteins that contain classical nuclear localization sequences (NLS) and, in complex with importin-β, is able to translocate nuclear proteins through the nuclear pore complex. The filamentous fungusNeurospora crassais a well studied organism that has been widely used as a model organism for fundamental aspects of eukaryotic biology, and is important for understanding the specific mechanisms of protein transport to the cell nucleus. In this work, the crystallization and preliminary X-ray diffraction analysis of importin-α fromN. crassa(IMPα-Nc) complexed with a classical NLS peptide (SV40 NLS) are reported. IMPα-Nc–SV40 NLS crystals diffracted X-rays to 2.0 Å resolution and the structure was solved by molecular-replacement techniques, leading to a monomeric structure. The observation of the electron-density map indicated the presence of SV40 NLSs interacting at both the minor and major NLS-binding sites of the protein. |
| Databáze: | OpenAIRE |
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