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

Marcos R M Fontes; Trazel Teh; Ryan D Riell; Seung Bum Park; Robert F Standaert; Bostjan Kobe

doi:10.1016/j.bbapap.2005.03.014

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

Biochim Biophys Acta. 2005 Jun 15;1750(1):9-13. doi: 10.1016/j.bbapap.2005.03.014. Epub 2005 Apr 13.

Authors

Marcos R M Fontes¹, Trazel Teh, Ryan D Riell, Seung Bum Park, Robert F Standaert, Bostjan Kobe

Affiliation

¹ Departamento de Física e Biofísica, Instituto de Biociências, UNESP, C. P. 510, CEP 18618-000, Botucatu-SP, Brazil. [email protected]

PMID: 15878698
DOI: 10.1016/j.bbapap.2005.03.014

Abstract

Importin-alpha is the nuclear import receptor that recognizes cargo proteins with nuclear localization sequences (NLSs). The 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-alpha was crystallized with a set of six NLS peptidomimetics, and X-ray diffraction data were collected in the range 2.1-2.5 A resolution. Preliminary electron density calculations show that the ligands are present in the crystals.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Models, Molecular
Molecular Mimicry*
Nuclear Localization Signals / chemistry*
Nuclear Localization Signals / metabolism
Protein Conformation
X-Ray Diffraction
alpha Karyopherins / chemistry*
alpha Karyopherins / metabolism*

Substances

Nuclear Localization Signals
alpha Karyopherins