3vyx

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Structural insights into RISC assembly facilitated by dsRNA binding domains of human RNA helicase (DHX9)Structural insights into RISC assembly facilitated by dsRNA binding domains of human RNA helicase (DHX9)

Structural highlights

3vyx is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.29Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHX9_HUMAN Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alteration of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Component of the CRD-mediated complex that promotes MYC mRNA stability. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms. Positively regulates HIV-1 LTR-directed gene expression.[1] [2] [3]

See Also

References

  1. Weidensdorfer D, Stohr N, Baude A, Lederer M, Kohn M, Schierhorn A, Buchmeier S, Wahle E, Huttelmaier S. Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs. RNA. 2009 Jan;15(1):104-15. doi: 10.1261/rna.1175909. Epub 2008 Nov 24. PMID:19029303 doi:10.1261/rna.1175909
  2. Sadler AJ, Latchoumanin O, Hawkes D, Mak J, Williams BR. An antiviral response directed by PKR phosphorylation of the RNA helicase A. PLoS Pathog. 2009 Feb;5(2):e1000311. doi: 10.1371/journal.ppat.1000311. Epub 2009, Feb 20. PMID:19229320 doi:http://dx.doi.org/10.1371/journal.ppat.1000311
  3. Manojlovic Z, Stefanovic B. A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs. RNA. 2012 Feb;18(2):321-34. doi: 10.1261/rna.030288.111. Epub 2011 Dec 21. PMID:22190748 doi:http://dx.doi.org/10.1261/rna.030288.111

3vyx, resolution 2.29Å

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OCA