|
|
| Line 1: |
Line 1: |
| | | | |
| | ==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <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 [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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> | + | <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><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2rs7|2rs7]], [[1whq|1whq]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dhx9, Ddx9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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> | + | |
| | </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).
| + | [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 == |
| Line 28: |
Line 25: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: RNA helicase]]
| + | [[Category: Inoue M]] |
| - | [[Category: Inoue, M]] | + | [[Category: Kigawa T]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Muto Y]] |
| - | [[Category: Muto, Y]] | + | [[Category: Nagata T]] |
| - | [[Category: Nagata, T]] | + | [[Category: Shirouzu M]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Terada T]] |
| - | [[Category: Shirouzu, M]] | + | [[Category: Tsuda K]] |
| - | [[Category: Terada, T]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Tsuda, K]] | + | |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Double-stranded rna binding domain]]
| + | |
| - | [[Category: Dsrbd]]
| + | |
| - | [[Category: Dsrm]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| 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
|
