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Cloning, expression, purification and preliminary crystallographic studies of the adenylate/uridylate‐rich element‐binding protein HuR complexed with its target RNA

Cloning, expression, purification and preliminary crystallographic studies of the... Adenylate/uridylate‐rich elements (AREs), which are found in the 3′‐untranslated region (UTR) of many mRNAs, influence the stability of cytoplasmic mRNA. HuR (human antigen R) binds to AREs and regulates various genes. In order to reveal the RNA‐recognition mechanism of HuR protein, an RNA‐binding region of human HuR containing two N‐terminal RNA‐recognition motif domains bound to an 11‐base RNA fragment has been crystallized. The crystals belonged to space group P212121, with unit‐cell parameters a = 42.4, b = 44.9, c = 91.1 Å. X‐ray diffraction data were collected to 1.8 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Cloning, expression, purification and preliminary crystallographic studies of the adenylate/uridylate‐rich element‐binding protein HuR complexed with its target RNA

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References (17)

Publisher
Wiley
Copyright
International Union of Crystallography, 2009
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430910900400X
pmid
19255485
Publisher site
See Article on Publisher Site

Abstract

Adenylate/uridylate‐rich elements (AREs), which are found in the 3′‐untranslated region (UTR) of many mRNAs, influence the stability of cytoplasmic mRNA. HuR (human antigen R) binds to AREs and regulates various genes. In order to reveal the RNA‐recognition mechanism of HuR protein, an RNA‐binding region of human HuR containing two N‐terminal RNA‐recognition motif domains bound to an 11‐base RNA fragment has been crystallized. The crystals belonged to space group P212121, with unit‐cell parameters a = 42.4, b = 44.9, c = 91.1 Å. X‐ray diffraction data were collected to 1.8 Å resolution.

Journal

Acta Crystallographica Section FWiley

Published: Mar 1, 2009

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