4CH0
RRM domain from C. elegans SUP-12
Summary for 4CH0
| Entry DOI | 10.2210/pdb4ch0/pdb |
| Related | 4CH1 4CIO |
| NMR Information | BMRB: 18845 |
| Descriptor | PROTEIN SUP-12, ISOFORM B (1 entity in total) |
| Functional Keywords | transcription, development |
| Biological source | CAENORHABDITIS ELEGANS |
| Total number of polymer chains | 1 |
| Total formula weight | 10831.20 |
| Authors | Amrane, S.,Mackereth, C.D. (deposition date: 2013-11-27, release date: 2014-09-03, Last modification date: 2024-05-15) |
| Primary citation | Amrane, 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: 25183497DOI: 10.1038/NCOMMS5595 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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