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1P27

Crystal Structure of the Human Y14/Magoh complex

Summary for 1P27
Entry DOI10.2210/pdb1p27/pdb
DescriptorMago nashi protein homolog, RNA-binding protein 8A (3 entities in total)
Functional Keywordsrna-binding, nuclear protein, mrna splicing, rna binding protein
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: P61326 Q9Y5S9
Total number of polymer chains4
Total formula weight58167.12
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 citationLau, 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: 12781131
DOI: 10.1016/S0960-9822(03)00328-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

246031

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