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Solution structures of the double‐stranded RNA‐binding domains from rna helicase A
Author(s) -
Nagata Takashi,
Tsuda Kengo,
Kobayashi Naohiro,
Shirouzu Mikako,
Kigawa Takanori,
Güntert Peter,
Yokoyama Shigeyuki,
Muto Yutaka
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24059
Subject(s) - rna , ribonucleoprotein , rna helicase a , helicase , microbiology and biotechnology , dna , rna binding protein , computational biology , chemistry , biology , gene , biochemistry
RNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex. We present the first solution structures of the double‐stranded RNA‐binding domains (dsRBDs), dsRBD1 and dsRBD2, from mouse RHA. We discuss the binding mode of the dsRBDs of RHA, in comparison with the known dsRBD structures in their complexes. Our structural data provide important information for the elucidation of the molecular reassembly mediated by RHA. Proteins 2012;. © 2012 Wiley Periodicals, Inc.