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

被引：2
|
作者：
Fontes, MRM
Teh, T
Riell, RD
Park, SB
Standaert, RE
Kobe, B
机构：
[1] Univ Estadual Paulista, Dept Fis & Biofis, Inst Biociencias, BR-18618000 Botucatu, SP, Brazil
[2] Univ Queensland, Dept Biochem & Mol Biol, Inst Mol Biosci, ARC Special Res Ctr Funct & Appl Genom, Brisbane, Qld 4072, Australia
[3] Univ Queensland, Cooperat Res Ctr Chron Inflammatory Dis, Brisbane, Qld 4072, Australia
[4] Univ Illinois, Dept Chem, Chicago, IL USA
[5] Seoul Natl Univ, Sch Chem, Seoul 151742, South Korea
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2005年 / 1750卷 / 01期
基金：
巴西圣保罗研究基金会;
关键词：
crystallization; X-ray crystallography; importin-alpha; karyopherin-alpha; nuclear localization sequence; NLS peptidomimetic ligand;
D O I：
10.1016/j.bbapap.2005.03.014
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：9 / 13
页数：5
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