1P27
Crystal Structure of the Human Y14/Magoh complex
Summary for 1P27
| Entry DOI | 10.2210/pdb1p27/pdb |
| Descriptor | Mago nashi protein homolog, RNA-binding protein 8A (3 entities in total) |
| Functional Keywords | rna-binding, nuclear protein, mrna splicing, rna binding protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P61326 Q9Y5S9 |
| Total number of polymer chains | 4 |
| Total formula weight | 58167.12 |
| Authors | Lau, C.K.,Diem, M.D.,Dreyfuss, G.,Van Duyne, G.D. (deposition date: 2003-04-14, release date: 2003-08-19, Last modification date: 2024-02-14) |
| Primary citation | Lau, C.K.,Diem, M.D.,Dreyfuss, G.,Van Duyne, G.D. Structure of the y14-magoh core of the exon junction complex. Curr.Biol., 13:933-941, 2003 Cited by PubMed Abstract: Splicing of pre-mRNA in eukaryotes imprints the resulting mRNA with a specific multiprotein complex, the exon-exon junction complex (EJC), at the sites of intron removal. The proteins of the EJC, Y14, Magoh, Aly/REF, RNPS1, Srm160, and Upf3, play critical roles in postsplicing processing, including nuclear export and cytoplasmic localization of the mRNA, and the nonsense-mediated mRNA decay (NMD) surveillance process. Y14 and Magoh are of particular interest because they remain associated with the mRNA in the same position after its export to the cytoplasm and require translation of the mRNA for removal. This tenacious, persistent, splicing-dependent, yet RNA sequence-independent, association suggests an important signaling function and must require distinct structural features for these proteins. PubMed: 12781131DOI: 10.1016/S0960-9822(03)00328-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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