This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3v53

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:11, 25 December 2014

Crystal structure of human RBM25

Structural highlights

3v53 is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	RBM25 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhou A, Ou AC, Cho A, Benz EJ Jr, Huang SC. Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection. Mol Cell Biol. 2008 Oct;28(19):5924-36. doi: 10.1128/MCB.00560-08. Epub 2008 Jul , 28. PMID:18663000 doi:10.1128/MCB.00560-08
↑ Gong D, Yang F, Li F, Qian D, Wu M, Shao Z, Wu M, Wu J, Shi Y. Crystal structure and functional characterization of the human RBM25 PWI domain and its flanking basic region. Biochem J. 2012 Nov 28. PMID:23190262 doi:10.1042/BJ20121382

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3v53"

Categories: Homo sapiens | Gong, D S | Pwi | Rna binding protein | Rna-binding domain

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v53 RCSB], [http://www.ebi.ac.uk/pdbsum/3v53 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==

3v53

From Proteopedia

Revision as of 04:11, 25 December 2014

Crystal structure of human RBM25

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox