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2I2Y

Solution structure of the RRM of SRp20 bound to the RNA CAUC

Summary for 2I2Y
Entry DOI10.2210/pdb2i2y/pdb
Descriptor(5'-R(*CP*AP*UP*C)-3'), Fusion protein consists of immunoglobulin G-Binding Protein G and Splicing factor, arginine/serine-rich 3 (2 entities in total)
Functional Keywordsprotein-rna complex rrm alpha-beta sandwich beta1-alpha1-beta2-beta3-alpha2-beta4, rna binding protein-chimera-rna complex, rna binding protein/chimera/rna
Biological sourceStreptococcus sp. 'group G', Homo sapiens (, human)
Cellular locationNucleus: P84103
Total number of polymer chains2
Total formula weight18061.46
Authors
Hargous, Y.F.,Allain, F.H. (deposition date: 2006-08-17, release date: 2006-12-12, Last modification date: 2024-05-29)
Primary citationHargous, Y.,Hautbergue, G.M.,Tintaru, A.M.,Skrisovska, L.,Golovanov, A.P.,Stevenin, J.,Lian, L.Y.,Wilson, S.A.,Allain, F.H.
Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8.
Embo J., 25:5126-5137, 2006
Cited by
PubMed Abstract: The sequence-specific RNA-binding proteins SRp20 and 9G8 are the smallest members of the serine- and arginine-rich (SR) protein family, well known for their role in splicing. They also play a role in mRNA export, in particular of histone mRNAs. We present the solution structures of the free 9G8 and SRp20 RNA recognition motifs (RRMs) and of SRp20 RRM in complex with the RNA sequence 5'CAUC3'. The SRp20-RNA structure reveals that although all 4 nt are contacted by the RRM, only the 5' cytosine is primarily recognized in a specific way. This might explain the numerous consensus sequences found by SELEX (systematic evolution of ligands by exponential enrichment) for the RRM of 9G8 and SRp20. Furthermore, we identify a short arginine-rich peptide adjacent to the SRp20 and 9G8 RRMs, which does not contact RNA but is necessary and sufficient for interaction with the export factor Tip-associated protein (TAP). Together, these results provide a molecular description for mRNA and TAP recognition by SRp20 and 9G8.
PubMed: 17036044
DOI: 10.1038/sj.emboj.7601385
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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