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


Autoria(s): Fontes, MRM; Teh, T.; Riell, R. D.; Park, S. B.; Standaert, R. E.; Kobe, B.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

15/06/2005

Resumo

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.

Formato

9-13

Identificador

http://dx.doi.org/10.1016/j.bbapap.2005.03.014

Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1750, n. 1, p. 9-13, 2005.

1570-9639

http://hdl.handle.net/11449/17561

10.1016/j.bbapap.2005.03.014

WOS:000229810800003

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Biochimica et Biophysica Acta: Proteins and Proteomics

Direitos

closedAccess

Palavras-Chave #crystallization #X-ray crystallography #importin-alpha #karyopherin-alpha #nuclear localization sequence #NLS peptidomimetic ligand
Tipo

info:eu-repo/semantics/article