Crystallization and preliminary X-ray crystallographic analysis of importin-alpha from Neurospora crassa
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
03/12/2014
03/12/2014
01/04/2014
|
Resumo |
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Importin-alpha recognizes cargo proteins that contain classical nuclear localization sequences (NLS) and, in complex with importin-beta, 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-alpha from N. crassa (IMP alpha-Nc) complexed with a classical NLS peptide (SV40 NLS) are reported. IMP alpha-Nc-SV40 NLS crystals diffracted X-rays to 2.0 angstrom 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. |
Formato |
501-504 |
Identificador |
http://dx.doi.org/10.1107/S2053230X14005068 Acta Crystallographica Section F-structural Biology Communications. Hoboken: Wiley-blackwell, v. 70, p. 501-504, 2014. 1744-3091 http://hdl.handle.net/11449/112614 10.1107/S2053230X14005068 WOS:000333757800022 |
Idioma(s) |
eng |
Publicador |
Wiley-Blackwell |
Relação |
Acta Crystallographica Section F: Structural Biology Communications |
Direitos |
closedAccess |
Tipo |
info:eu-repo/semantics/article |