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Crystallization and preliminary X-ray crystallographic analysis of importin-α from Neurospora crassa.

Research paper by Natalia E NE Bernardes, Agnes A S AA Takeda, Fernanda Z FZ Freitas, Maria Célia MC Bertolini, Marcos R M MR Fontes

Indexed on: 05 Apr '14Published on: 05 Apr '14Published in: Acta Crystallographica Section F



Abstract

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 fungus Neurospora crassa is 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 from N. 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.

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