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4CH1

RRM domain from C. elegans SUP-12 bound to GGTGTGC DNA

Summary for 4CH1
Entry DOI10.2210/pdb4ch1/pdb
Related4CH0
NMR InformationBMRB: 19653
DescriptorPROTEIN SUP-12, ISOFORM B, GGTGTGC (2 entities in total)
Functional Keywordstranscription-dna complex, muscle, development, transcription/dna
Biological sourceCAENORHABDITIS ELEGANS
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Total number of polymer chains2
Total formula weight13000.63
Authors
Amrane, S.,Mackereth, C.D. (deposition date: 2013-11-28, release date: 2014-09-03, Last modification date: 2024-05-15)
Primary citationAmrane, S.,Rebora, K.,Zniber, I.,Dupuy, D.,Mackereth, C.D.
Backbone-Independent Nucleic Acid Binding by Splicing Factor Sup-12 Reveals Key Aspects of Molecular Recognition
Nat.Commun., 5:4595-, 2014
Cited by
PubMed Abstract: Cellular differentiation is frequently accompanied by alternative splicing, enabled by the expression of tissue-specific factors which bind to pre-mRNAs and regulate exon choice. During Caenorhabditis elegans development, muscle-specific expression of the splicing factor SUP-12, together with a member of the Fox-1 family of splicing proteins, generates a functionally distinct isoform of the fibroblast growth factor receptor EGL-15. Using a combination of NMR spectroscopy and isothermal titration calorimetry, we determined the mode of nucleic acid binding by the RNA recognition motif domain of SUP-12. The calculated structures provide the first atomic details of RNA and DNA binding by the family of proteins that include SUP-12, RBM24, RBM38/RNPC1, SEB-4 and XSeb4R. This information was further used to design strategic mutations to probe the interaction with ASD-1 and to quantitatively perturb splicing in vivo.
PubMed: 25183497
DOI: 10.1038/NCOMMS5595
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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