2ymj

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Template:STRUCTURE 2ymj

Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.

Template:ABSTRACT PUBMED 23520467

FunctionFunction

[QKIA_XENLA] RNA-binding protein that plays a central role in myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation. Required to protect and promote stability of mRNAs which promotes oligodendrocyte differentiation. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of some pre-mRNA. Acts as a translational repressor (By similarity). Essential for notochord development.[1]

About this StructureAbout this Structure

2ymj is a 1 chain structure with sequence from Xenopus laevis. Full experimental information is available from OCA.

ReferenceReference

[xtra 1]

  1. Ali M, Broadhurst RW. Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking. PLoS One. 2013;8(3):e57345. doi: 10.1371/journal.pone.0057345. Epub 2013 Mar 8. PMID:23520467 doi:http://dx.doi.org/10.1371/journal.pone.0057345
  1. Zorn AM, Krieg PA. The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos. Genes Dev. 1997 Sep 1;11(17):2176-90. PMID:9303534

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