View source for 5mf9


==Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide.==
<StructureSection load='5mf9' size='340' side='right'caption='[[5mf9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mf9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MF9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5mf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mf9 OCA], [https://pdbe.org/5mf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mf9 RCSB], [https://www.ebi.ac.uk/pdbsum/5mf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mf9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBM5_HUMAN RBM5_HUMAN] Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis.<ref>PMID:10949932</ref> <ref>PMID:12207175</ref> <ref>PMID:12581154</ref> <ref>PMID:15192330</ref> <ref>PMID:16585163</ref> <ref>PMID:18851835</ref> <ref>PMID:18840686</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The multi-domain splicing factor RBM5 regulates the balance between antagonistic isoforms of the apoptosis-control genes FAS/CD95, Caspase-2 and AID. An OCRE (OCtamer REpeat of aromatic residues) domain found in RBM5 is important for alternative splicing regulation and mediates interactions with components of the U4/U6.U5 tri-snRNP. We show that the RBM5 OCRE domain adopts a unique beta-sheet fold. NMR and biochemical experiments demonstrate that the OCRE domain directly binds to the proline-rich C-terminal tail of the essential snRNP core proteins SmN/B/B'. The NMR structure of an OCRE-SmN peptide complex reveals a specific recognition of poly-proline helical motifs in SmN/B/B'. Mutation of conserved aromatic residues impairs binding to the Sm proteins in vitro and compromises RBM5-mediated alternative splicing regulation of FAS/CD95. Thus, RBM5 OCRE represents a poly-proline recognition domain that mediates critical interactions with the C-terminal tail of the spliceosomal SmN/B/B' proteins in FAS/CD95 alternative splicing regulation.

Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation.,Mourao A, Bonnal S, Soni K, Warner L, Bordonne R, Valcarcel J, Sattler M Elife. 2016 Nov 29;5. pii: e14707. doi: 10.7554/eLife.14707. PMID:27894420<ref>PMID:27894420</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mf9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bonnal S]]
[[Category: Bordonne R]]
[[Category: Komal S]]
[[Category: Mourao A]]
[[Category: Sattler M]]
[[Category: Valcarcel J]]
[[Category: Warner L]]