2KXN

NMR structure of human Tra2beta1 RRM in complex with AAGAAC RNA


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 12 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

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, F.H.

(2011) Nat Struct Mol Biol 18: 443-450

  • DOI: https://doi.org/10.1038/nsmb.2001
  • Primary Citation of Related Structures:  
    2KXN

  • 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.


  • Organizational Affiliation

    Institute for Molecular Biology and Biophysics, Swiss Federal Institute of Technology, Zürich, Switzerland.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Transformer-2 protein homolog beta129Homo sapiensMutation(s): 0 
Gene Names: TRA2BSFRS10
UniProt & NIH Common Fund Data Resources
Find proteins for P62995 (Homo sapiens)
Explore P62995 
Go to UniProtKB:  P62995
PHAROS:  P62995
GTEx:  ENSG00000136527 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP62995
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-R(*AP*AP*GP*AP*AP*C)-3'6N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 12 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-03-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2012-05-30
    Changes: Database references
  • Version 1.3: 2020-02-05
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-05-01
    Changes: Data collection, Database references