3v53

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Crystal structure of human RBM25

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Categories: Homo sapiens | Large Structures | Gong DS

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 <StructureSection load='3v53' size='340' side='right'caption='[[3v53]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3v53]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3v53]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V53 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RBM25 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=3v53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v53 OCA], [https://pdbe.org/3v53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v53 RCSB], [https://www.ebi.ac.uk/pdbsum/3v53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v53 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RBM25_HUMAN RBM25_HUMAN]] RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA.<ref>PMID:18663000</ref>
+[https://www.uniprot.org/uniprot/RBM25_HUMAN RBM25_HUMAN] RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression. Modulates the ratio of proapoptotic BCL2L1 isoform S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA.<ref>PMID:18663000</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Human RBM25 (RNA-binding protein 25) is a novel splicing factor that contains a PWI domain, a newly identified RNA/DNA-binding domain, and regulates Bcl-x pre-mRNA alternative splicing. The flanking basic region has been suggested to serve as a cooperative partner of the PWI domain in the binding of nucleic acids, but the structure of this basic region is unknown. Here, we report the crystal structure of the RBM25 PWI domain and its flanking basic region. The PWI domain is revealed to comprise a conserved four-helix bundle, and the flanking basic region forms two alpha-helices and associates with helix H4 of the PWI domain. These interactions directly promote the formation of an enlarged nucleic acid-binding platform. Structure-guided mutagenesis reveals a positive charged nucleic acid-binding surface in the RBM25 PWI domain that is entirely different from that in the SRm160 PWI domain. Furthermore, we show that the promotion of the proapoptotic Bcl-x(s) isoform expression by RBM25 is facilitated by the PWI domain in vivo. Thus, our study suggests that the PWI domain plays an important role in the regulation of Bcl-x pre-mRNA alternative splicing.
-Crystal structure and functional characterization of the human RBM25 PWI domain and its flanking basic region.,Gong D, Yang F, Li F, Qian D, Wu M, Shao Z, Wu M, Wu J, Shi Y Biochem J. 2012 Nov 28. PMID:23190262<ref>PMID:23190262</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3v53" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Gong, D S]]
+[[Category: Gong DS]]
-[[Category: Pwi]]
-[[Category: Rna binding protein]]
-[[Category: Rna-binding domain]]

3v53

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Crystal structure of human RBM25

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