6BJV
CIRV p19 protein in complex with siRNA
6BJV の概要
| エントリーDOI | 10.2210/pdb6bjv/pdb |
| 分子名称 | RNA silencing suppressor p19, RNA (5'-R(P*UP*CP*GP*AP*AP*GP*UP*AP*UP*UP*CP*CP*GP*CP*GP*UP*AP*CP*GP*UP*U)-3'), RNA (5'-R(P*CP*GP*UP*AP*CP*GP*CP*GP*GP*AP*AP*UP*AP*CP*UP*UP*CP*GP*AP*UP*U)-3'), ... (4 entities in total) |
| 機能のキーワード | viral suppressor, rna silencing sirna binding protein p19, altered affinity for microrna, rna binding protein |
| 由来する生物種 | Carnation Italian ringspot virus (CIRV) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 52073.71 |
| 構造登録者 | Foss, D.V.,Schirle, N.,Pezacki, J.P.,Macrae, I.J. (登録日: 2017-11-07, 公開日: 2019-01-16, 最終更新日: 2023-10-04) |
| 主引用文献 | Foss, D.V.,Schirle, N.T.,MacRae, I.J.,Pezacki, J.P. Structural insights into interactions between viral suppressor of RNA silencing protein p19 mutants and small RNAs. Febs Open Bio, 9:1042-1051, 2019 Cited by PubMed Abstract: Viral suppressors of RNA silencing (VSRSs) are a diverse group of viral proteins that have evolved to disrupt eukaryotic RNA silencing pathways, thereby contributing to viral pathogenicity. The p19 protein is a VSRS that selectively binds to short interfering RNAs (siRNAs) over microRNAs (miRNAs). Mutational analysis has identified single amino acid substitutions that reverse this selectivity through new high-affinity interactions with human miR-122. Herein, we report crystal structures of complexed p19-T111S (2.6 Å), p19-T111H (2.3 Å) and wild-type p19 protein (2.2 Å) from the Carnation Italian ringspot virus with small interfering RNA (siRNA) ligands. Structural comparisons reveal that these mutations do not lead to major changes in p19 architecture, but instead promote subtle rearrangement of residues and solvent molecules along the p19 midline. These observations suggest p19 uses many small interactions to distinguish siRNAs from miRNAs and perturbing these interactions can create p19 variants with novel RNA-recognition properties. DATABASE: Model data are deposited in the PDB database under the accession numbers 6BJG, 6BJH and 6BJV. PubMed: 31021526DOI: 10.1002/2211-5463.12644 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.198 Å) |
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