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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/TRA2B_HUMAN TRA2B_HUMAN] Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA.<ref>PMID:9546399</ref> <ref>PMID:12165565</ref> <ref>PMID:12761049</ref> <ref>PMID:15009664</ref>  
[https://www.uniprot.org/uniprot/TRA2B_HUMAN TRA2B_HUMAN] Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA.<ref>PMID:9546399</ref> <ref>PMID:12165565</ref> <ref>PMID:12761049</ref> <ref>PMID:15009664</ref>  
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== Publication Abstract from PubMed ==
Tra2-beta1 is a unique splicing factor as its single RNA recognition motif (RRM) is located between two RS (arginine-serine) domains. To understand how this protein recognizes its RNA target, we solved the structure of Tra2-beta1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the beta-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-beta1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-beta1 and RNA mutations on the splicing of SMN2 exon 7, we validated the importance of the RNA-protein contacts observed in the structure for the function of Tra2-beta1 and determined the functional sequence of Tra2-beta1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.
Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1.,Clery A, Jayne S, Benderska N, Dominguez C, Stamm S, Allain FH Nat Struct Mol Biol. 2011 Apr;18(4):443-50. Epub 2011 Mar 13. PMID:21399644<ref>PMID:21399644</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Latest revision as of 06:50, 1 May 2024

NMR structure of human Tra2beta1 RRM in complex with AAGAAC RNA

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