1HL6
A novel mode of RBD-protein recognition in the Y14-mago complex
Summary for 1HL6
| Entry DOI | 10.2210/pdb1hl6/pdb |
| Descriptor | CG8781 PROTEIN, MAGO NASHI PROTEIN (3 entities in total) |
| Functional Keywords | signal protein, rdb, exon-exon junction, oskar, rnp, nmd |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) More |
| Total number of polymer chains | 4 |
| Total formula weight | 73264.46 |
| Authors | Fribourg, S.,Gatfield, D.,Yao, W.,Izaurralde, E.,Conti, E. (deposition date: 2003-03-13, release date: 2003-05-08, Last modification date: 2024-05-08) |
| Primary citation | Fribourg, S.,Gatfield, D.,Izaurralde, E.,Conti, E. A Novel Mode of Rbd-Protein Recognition in the Y14-Mago Complex Nat.Struct.Biol., 10:433-, 2003 Cited by PubMed Abstract: Y14 and Mago are conserved eukaryotic proteins that associate with spliced mRNAs in the nucleus and remain associated at exon junctions during and after nuclear export. In the cytoplasm, Y14 is involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway and, together with Mago, is involved in localization of osk (oskar) mRNA. We have determined the crystal structure of the complex between Drosophila melanogaster Y14 and Mago at a resolution of 2.5 A. The structure reveals an atypical mode of protein-protein recognition mediated by an RNA-binding domain (RBD). Instead of binding RNA, the RBD of Y14 engages its RNP1 and RNP2 motifs to bind Mago. Using structure-guided mutagenesis, we show that Mago is also a component of the NMD pathway, and that its association with Y14 is essential for function. Heterodimerization creates a single structural platform that interacts with the NMD machinery via phylogenetically conserved residues. PubMed: 12730685DOI: 10.1038/NSB926 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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