You are in the accessibility menu

Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/17561
Title: 
Crystallization and preliminary X-ray diffraction analysis of importin-alpha acomplexed with NLS peptidomimetics
Author(s): 
Institution: 
  • Universidade Estadual Paulista (UNESP)
  • Univ Queensland
  • Univ Illinois
  • Seoul Natl Univ
ISSN: 
1570-9639
Abstract: 
Importin-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.
Issue Date: 
15-Jun-2005
Citation: 
Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1750, n. 1, p. 9-13, 2005.
Time Duration: 
9-13
Publisher: 
Elsevier B.V.
Keywords: 
  • crystallization
  • X-ray crystallography
  • importin-alpha
  • karyopherin-alpha
  • nuclear localization sequence
  • NLS peptidomimetic ligand
Source: 
http://dx.doi.org/10.1016/j.bbapap.2005.03.014
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/17561
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.
 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.