1p27
From Proteopedia
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Crystal Structure of the Human Y14/Magoh complex
Overview
BACKGROUND: 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. RESULTS: We describe the, high-resolution structure and biochemical properties of the highly, conserved human Y14 and Magoh proteins. Magoh has an unusual structure, comprised of an extremely flat, six-stranded anti-parallel beta sheet, packed against two helices. Surprisingly, Magoh binds with high affinity, to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its, RNA binding surface. CONCLUSIONS: The structure and properties of the, Y14-Magoh complex suggest how the pre-mRNA splicing machinery might, control the formation of a stable EJC-mRNA complex at splice junctions.
About this Structure
1P27 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Y14-Magoh core of the exon junction complex., Lau CK, Diem MD, Dreyfuss G, Van Duyne GD, Curr Biol. 2003 May 27;13(11):933-41. PMID:12781131
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