2ru3: Difference between revisions
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==Solution structure of c.elegans SUP-12 RRM in complex with RNA== | ==Solution structure of c.elegans SUP-12 RRM in complex with RNA== | ||
<StructureSection load='2ru3' size='340' side='right' caption='[[2ru3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2ru3' size='340' side='right'caption='[[2ru3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ru3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ru3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RU3 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mgz|2mgz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mgz|2mgz]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sup-12, CELE_T22B2.4, T22B2.4 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sup-12, CELE_T22B2.4, T22B2.4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ru3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru3 OCA], [https://pdbe.org/2ru3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ru3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ru3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Caeel]] | [[Category: Caeel]] | ||
[[Category: Large Structures]] | |||
[[Category: Guntert, P]] | [[Category: Guntert, P]] | ||
[[Category: Hagiwara, M]] | [[Category: Hagiwara, M]] |
Revision as of 13:36, 7 July 2021
Solution structure of c.elegans SUP-12 RRM in complex with RNASolution structure of c.elegans SUP-12 RRM in complex with RNA
Structural highlights
Publication Abstract from PubMedTissue-specific alternative pre-mRNA splicing is often cooperatively regulated by multiple splicing factors, but the structural basis of cooperative RNA recognition is poorly understood. In Caenorhabditis elegans, ligand binding specificity of fibroblast growth factor receptors (FGFRs) is determined by mutually exclusive alternative splicing of the sole FGFR gene, egl-15. Here we determined the solution structure of a ternary complex of the RNA-recognition motif (RRM) domains from the RBFOX protein ASD-1, SUP-12 and their target RNA from egl-15. The two RRM domains cooperatively interact with the RNA by sandwiching a G base to form the stable complex. Multichromatic fluorescence splicing reporters confirmed the requirement of the G and the juxtaposition of the respective cis elements for effective splicing regulation in vivo. Moreover, we identified a new target for the heterologous complex through an element search, confirming the functional significance of the intermolecular coordination. RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing.,Kuwasako K, Takahashi M, Unzai S, Tsuda K, Yoshikawa S, He F, Kobayashi N, Guntert P, Shirouzu M, Ito T, Tanaka A, Yokoyama S, Hagiwara M, Kuroyanagi H, Muto Y Nat Struct Mol Biol. 2014 Sep;21(9):778-86. doi: 10.1038/nsmb.2870. Epub 2014 Aug, 17. PMID:25132178[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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