4cio: Difference between revisions
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New page: '''Unreleased structure''' The entry 4cio is ON HOLD until sometime in the future Authors: Amrane, S., Mackereth, C.D. Description: RRM domain from C. elegans SUP-12 bound to GGUGUGC R... |
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==RRM domain from C. elegans SUP-12 bound to GGUGUGC RNA== | |||
<StructureSection load='4cio' size='340' side='right'caption='[[4cio]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4cio]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CIO FirstGlance]. <br> | |||
</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=4cio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cio OCA], [https://pdbe.org/4cio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cio RCSB], [https://www.ebi.ac.uk/pdbsum/4cio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cio ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/O45189_CAEEL O45189_CAEEL]] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cellular differentiation is frequently accompanied by alternative splicing, enabled by the expression of tissue-specific factors which bind to pre-mRNAs and regulate exon choice. During Caenorhabditis elegans development, muscle-specific expression of the splicing factor SUP-12, together with a member of the Fox-1 family of splicing proteins, generates a functionally distinct isoform of the fibroblast growth factor receptor EGL-15. Using a combination of NMR spectroscopy and isothermal titration calorimetry, we determined the mode of nucleic acid binding by the RNA recognition motif domain of SUP-12. The calculated structures provide the first atomic details of RNA and DNA binding by the family of proteins that include SUP-12, RBM24, RBM38/RNPC1, SEB-4 and XSeb4R. This information was further used to design strategic mutations to probe the interaction with ASD-1 and to quantitatively perturb splicing in vivo. | |||
Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition.,Amrane S, Rebora K, Zniber I, Dupuy D, Mackereth CD Nat Commun. 2014 Sep 3;5:4595. doi: 10.1038/ncomms5595. PMID:25183497<ref>PMID:25183497</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cio" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | |||
[[Category: Amrane S]] | |||
[[Category: Mackereth CD]] | |||
Latest revision as of 07:17, 14 September 2022
RRM domain from C. elegans SUP-12 bound to GGUGUGC RNA
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