Open AccessPreliminary crystallographic analysis of the RNA‐binding domain of HuR and its poly(U)‐binding properties
Author(s) -
Wang Hong,
Li Heng,
Shi Hui,
Liu Yang,
Liu Huihui,
Zhao Hui,
Niu Liwen,
Teng Maikun,
Li Xu
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110052930
Subject(s) - recombinant dna , rna binding protein , rna , microbiology and biotechnology , chemistry , mutagenesis , crystallography , rna recognition motif , biology , biochemistry , gene , mutation
Human antigen R (HuR), a ubiquitously expressed member of the Hu protein family, is an important post‐transcriptional regulator which has three RNA‐recognition motif (RRM) domains. The two tandem N‐terminal RRM domains can selectively bind to the AU‐rich element (ARE), while the third one interacts with the poly(A) tail and other proteins. Here, the recombinant ARE‐binding region of HuR (residues 18–186) was crystallized in space group P 2 1 2 1 2, with unit‐cell parameters a = 41.2, b = 133.1, c = 31.4 Å. X‐ray diffraction data were collected to a resolution of 2.8 Å. Mutagenesis analysis and SPR assays revealed its poly(U)‐binding properties.