7VKI
ESRP1 qRRM2 in complex with 12mer-RNA
7VKI の概要
| エントリーDOI | 10.2210/pdb7vki/pdb |
| 分子名称 | Epithelial splicing regulatory protein 1, RNA (12-mer) (3 entities in total) |
| 機能のキーワード | qrrm domain, rna binding, circrna, complex, rna binding protein, rna binding protein-rna complex, rna binding protein/rna |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 17151.49 |
| 構造登録者 | |
| 主引用文献 | Liu, D.,Dredge, B.K.,Bert, A.G.,Pillman, K.A.,Toubia, J.,Guo, W.,Dyakov, B.J.A.,Migault, M.M.,Conn, V.M.,Conn, S.J.,Gregory, P.A.,Gingras, A.C.,Patel, D.,Wu, B.,Goodall, G.J. ESRP1 controls biogenesis and function of a large abundant multiexon circRNA. Nucleic Acids Res., 2023 Cited by PubMed Abstract: While the majority of circRNAs are formed from infrequent back-splicing of exons from protein coding genes, some can be produced at quite high level and in a regulated manner. We describe the regulation, biogenesis and function of circDOCK1(2-27), a large, abundant circular RNA that is highly regulated during epithelial-mesenchymal transition (EMT) and whose formation depends on the epithelial splicing regulator ESRP1. CircDOCK1(2-27) synthesis in epithelial cells represses cell motility both by diverting transcripts from DOCK1 mRNA production to circRNA formation and by direct inhibition of migration by the circRNA. HITS-CLIP analysis and CRISPR-mediated deletions indicate ESRP1 controls circDOCK1(2-27) biosynthesis by binding a GGU-containing repeat region in intron 1 and detaining its splicing until Pol II completes its 157 kb journey to exon 27. Proximity-dependent biotinylation (BioID) assay suggests ESRP1 may modify the RNP landscape of intron 1 in a way that disfavours communication of exon 1 with exon 2, rather than physically bridging exon 2 to exon 27. The X-ray crystal structure of RNA-bound ESRP1 qRRM2 domain reveals it binds to GGU motifs, with the guanines embedded in clamp-like aromatic pockets in the protein. PubMed: 38015468DOI: 10.1093/nar/gkad1138 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.65 Å) |
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