2rs6: Difference between revisions
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==Solution structure of the N-terminal dsRBD from RNA helicase A== | ==Solution structure of the N-terminal dsRBD from RNA helicase A== | ||
<StructureSection load='2rs6' size='340' side='right' caption='[[2rs6 | <StructureSection load='2rs6' size='340' side='right'caption='[[2rs6]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2rs6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2rs6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RS6 FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rs6 OCA], [https://pdbe.org/2rs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rs6 RCSB], [https://www.ebi.ac.uk/pdbsum/2rs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rs6 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DHX9_MOUSE 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). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Helicase|Helicase]] | *[[Helicase 3D structures|Helicase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Inoue | [[Category: Inoue M]] | ||
[[Category: Kigawa | [[Category: Kigawa T]] | ||
[[Category: Muto | [[Category: Muto Y]] | ||
[[Category: Nagata | [[Category: Nagata T]] | ||
[[Category: Shirouzu M]] | |||
[[Category: Shirouzu | [[Category: Terada T]] | ||
[[Category: Terada | [[Category: Tsuda K]] | ||
[[Category: Tsuda | [[Category: Yokoyama S]] | ||
[[Category: Yokoyama | |||
Latest revision as of 23:51, 12 April 2023
Solution structure of the N-terminal dsRBD from RNA helicase ASolution structure of the N-terminal dsRBD from RNA helicase A
Structural highlights
FunctionDHX9_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 PubMedRNA 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 AlsoReferences
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