2KXN

NMR structure of human Tra2beta1 RRM in complex with AAGAAC RNA

Summary for 2KXN

• Entry DOI: 10.2210/pdb2kxn/pdb
• NMR Information: BMRB: 16920
• Descriptor: 5'-R(*AP*AP*GP*AP*AP*C)-3', Transformer-2 protein homolog beta (2 entities in total)
• Functional Keywords: sr protein, rrm, splicing factor, rna protein complex, smn, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 16419.47

Authors

Clery, A.,Jayne, S.,Benderska, N.,Dominguez, C.,Stamm, S.,Allain, F.H.-T. (deposition date: 2010-05-10, release date: 2011-03-16, Last modification date: 2024-05-01)

Primary citation

Clery, A.,Jayne, S.,Benderska, N.,Dominguez, C.,Stamm, S.,Allain, F.H.
Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1
Nat.Struct.Mol.Biol., 18:443-450, 2011

PubMed Abstract: Tra2-β1 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-β1 RRM in complex with RNA. The central 5'-AGAA-3' motif is specifically recognized by residues from the β-sheet of the RRM and by residues from both extremities flanking the RRM. The structure suggests that RNA binding by Tra2-β1 induces positioning of the two RS domains relative to one another. By testing the effect of Tra2-β1 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-β1 and determined the functional sequence of Tra2-β1 in SMN2 exon 7. Finally, we propose a model for the assembly of multiple RNA binding proteins on this exon.

PubMed: 21399644
DOI: 10.1038/nsmb.2001

Experimental method

SOLUTION NMR