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