5UZN
Crystal structure of Glorund qRRM3 domain
Summary for 5UZN
| Entry DOI | 10.2210/pdb5uzn/pdb |
| Related | 5UZG 5UZM |
| Descriptor | AT27789p, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | quasi-rna recognition motif, qrrm, rna binding protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 11154.35 |
| Authors | Teramoto, T.,Hall, T.M.T. (deposition date: 2017-02-27, release date: 2017-03-29, Last modification date: 2023-10-04) |
| Primary citation | Tamayo, J.V.,Teramoto, T.,Chatterjee, S.,Hall, T.M.,Gavis, E.R. The Drosophila hnRNP F/H Homolog Glorund Uses Two Distinct RNA-Binding Modes to Diversify Target Recognition. Cell Rep, 19:150-161, 2017 Cited by PubMed Abstract: The Drosophila hnRNP F/H homolog, Glorund (Glo), regulates nanos mRNA translation by interacting with a structured UA-rich motif in the nanos 3' untranslated region. Glo regulates additional RNAs, however, and mammalian homologs bind G-tract sequences to regulate alternative splicing, suggesting that Glo also recognizes G-tract RNA. To gain insight into how Glo recognizes both structured UA-rich and G-tract RNAs, we used mutational analysis guided by crystal structures of Glo's RNA-binding domains and identified two discrete RNA-binding surfaces that allow Glo to recognize both RNA motifs. By engineering Glo variants that favor a single RNA-binding mode, we show that a subset of Glo's functions in vivo is mediated solely by the G-tract binding mode, whereas regulation of nanos requires both recognition modes. Our findings suggest a molecular mechanism for the evolution of dual RNA motif recognition in Glo that may be applied to understanding the functional diversity of other RNA-binding proteins. PubMed: 28380354DOI: 10.1016/j.celrep.2017.03.022 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
Download full validation report






