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2MGZ

Solution structure of RBFOX family ASD-1 RRM and SUP-12 RRM in ternary complex with RNA

Summary for 2MGZ
Entry DOI10.2210/pdb2mgz/pdb
Related2RU3
NMR InformationBMRB: 19609
DescriptorProtein ASD-1, isoform a, Protein SUP-12, isoform a, RNA (5'-R(*UP*GP*CP*AP*UP*GP*GP*UP*GP*UP*GP*C)-3') (3 entities in total)
Functional Keywordssolution structure, protein-rna complex, ternary complex, rrm (rna recognition motif), rna binding protein-rna complex, rna binding protein/rna
Biological sourceCaenorhabditis elegans (nematode)
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Total number of polymer chains3
Total formula weight26044.34
Authors
Primary citationKuwasako, K.,Takahashi, M.,Unzai, S.,Tsuda, K.,Yoshikawa, S.,He, F.,Kobayashi, N.,Guntert, P.,Shirouzu, M.,Ito, T.,Tanaka, A.,Yokoyama, S.,Hagiwara, M.,Kuroyanagi, H.,Muto, Y.
RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing
Nat.Struct.Mol.Biol., 21:778-786, 2014
Cited by
PubMed Abstract: Tissue-specific alternative pre-mRNA splicing is often cooperatively regulated by multiple splicing factors, but the structural basis of cooperative RNA recognition is poorly understood. In Caenorhabditis elegans, ligand binding specificity of fibroblast growth factor receptors (FGFRs) is determined by mutually exclusive alternative splicing of the sole FGFR gene, egl-15. Here we determined the solution structure of a ternary complex of the RNA-recognition motif (RRM) domains from the RBFOX protein ASD-1, SUP-12 and their target RNA from egl-15. The two RRM domains cooperatively interact with the RNA by sandwiching a G base to form the stable complex. Multichromatic fluorescence splicing reporters confirmed the requirement of the G and the juxtaposition of the respective cis elements for effective splicing regulation in vivo. Moreover, we identified a new target for the heterologous complex through an element search, confirming the functional significance of the intermolecular coordination.
PubMed: 25132178
DOI: 10.1038/nsmb.2870
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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