4CIO

RRM domain from C. elegans SUP-12 bound to GGUGUGC RNA

4CIO の概要

• エントリーDOI: 10.2210/pdb4cio/pdb
• 関連するPDBエントリー: 4CH0 4CH1
• NMR情報: BMRB: 18846
• 分子名称: PROTEIN SUP-12, ISOFORM A, 5'-R(*GP*GP*UP*GP*UP*GP*CP)-3' (2 entities in total)
• 機能のキーワード: rna binding protein-rna complex, muscle, development, rna binding protein/rna
• 由来する生物種: CAENORHABDITIS ELEGANS; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13084.58

構造登録者

Amrane, S.,Mackereth, C.D. (登録日: 2013-12-12, 公開日: 2014-09-03, 最終更新日: 2024-05-15)

主引用文献

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

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

実験手法

SOLUTION NMR