Structural highlights
Function
DHX9_MOUSE Component of the CRD-mediated complex that promotes MYC mRNA stability. Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alterations of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2 (By similarity).
Publication Abstract from PubMed
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.
Solution structures of the double-stranded RNA-binding domains from RNA helicase A.,Nagata T, Tsuda K, Kobayashi N, Shirouzu M, Kigawa T, Guntert P, Yokoyama S, Muto Y Proteins. 2012 Jun;80(6):1699-706. doi: 10.1002/prot.24059. Epub 2012 Mar 27. PMID:22454253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nagata T, Tsuda K, Kobayashi N, Shirouzu M, Kigawa T, Guntert P, Yokoyama S, Muto Y. Solution structures of the double-stranded RNA-binding domains from RNA helicase A. Proteins. 2012 Jun;80(6):1699-706. doi: 10.1002/prot.24059. Epub 2012 Mar 27. PMID:22454253 doi:http://dx.doi.org/10.1002/prot.24059
