Crystallization and preliminary X-ray diffraction analysis of importin-alpha acomplexed with NLS peptidomimetics

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniv Queensland
dc.contributorUniv Illinois
dc.contributorSeoul Natl Univ
dc.date.accessioned2014-05-20T13:49:18Z
dc.date.accessioned2022-10-05T14:20:35Z
dc.date.available2014-05-20T13:49:18Z
dc.date.available2022-10-05T14:20:35Z
dc.date.created2014-05-20T13:49:18Z
dc.date.issued2005-06-15
dc.identifierBiochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1750, n. 1, p. 9-13, 2005.
dc.identifier1570-9639
dc.identifierhttp://hdl.handle.net/11449/17561
dc.identifier10.1016/j.bbapap.2005.03.014
dc.identifierWOS:000229810800003
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3892232
dc.description.abstractImportin-alpha is the nuclear import receptor that recognizes cargo proteins with nuclear localization sequences (NLSs). Tile study of NLS peptidomimetics can provide a better understanding of the requirements for the molecular recognition of cargo proteins by importin-alpha, and potentially engender a large number of applications in medicine. Importin-a was crystallized with a set of six NLS peptidomimetics, and X-ray diffraction data were collected in the range 2.1-2.5 angstrom resolution. Preliminary electron density calculations show that the ligands are present in the crystals. (c) 2005 Elsevier B.V All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica et Biophysica Acta: Proteins and Proteomics
dc.relation2.609
dc.relation1,170
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectcrystallization
dc.subjectX-ray crystallography
dc.subjectimportin-alpha
dc.subjectkaryopherin-alpha
dc.subjectnuclear localization sequence
dc.subjectNLS peptidomimetic ligand
dc.titleCrystallization and preliminary X-ray diffraction analysis of importin-alpha acomplexed with NLS peptidomimetics
dc.typeArtigo


Este ítem pertenece a la siguiente institución