6SDW
Solution structure of Staufen1 dsRBD3+4 - hARF1 SBS dsRNA complex.
Summary for 6SDW
| Entry DOI | 10.2210/pdb6sdw/pdb |
| NMR Information | BMRB: 34421 |
| Descriptor | Double-stranded RNA-binding protein Staufen homolog 1, hARF1 SBS dsRNA (2 entities in total) |
| Functional Keywords | dsrbd-dsrna binding protein, staufen1 protein, staufen mediated mrna decay, nmr structure of rna-protein complex, rna binding protein, rna binding domain. |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 30670.60 |
| Authors | Yadav, D.K.,Lukavsky, P.J. (deposition date: 2019-07-29, release date: 2020-01-15, Last modification date: 2024-06-19) |
| Primary citation | Yadav, D.K.,Zigackova, D.,Zlobina, M.,Klumpler, T.,Beaumont, C.,Kubickova, M.,Vanacova, S.,Lukavsky, P.J. Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res., 48:2091-2106, 2020 Cited by PubMed Abstract: Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factor1 (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. Our structure of the ARF1 SBS-STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix α1, the β1-β2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix α2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection. PubMed: 31875226DOI: 10.1093/nar/gkz1163 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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