4cio
From Proteopedia
(Difference between revisions)
m (Protected "4cio" [edit=sysop:move=sysop]) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Current revision
RRM domain from C. elegans SUP-12 bound to GGUGUGC RNA
| |||||||||||
