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2X1G

Crystal structure of Importin13 - Mago-Y14 complex

Summary for 2X1G
Entry DOI10.2210/pdb2x1g/pdb
Related1HL6 1OO0 1RK8
DescriptorRNA-BINDING PROTEIN 8A, PROTEIN MAGO NASHI, CADMUS (3 entities in total)
Functional Keywordstransport protein, developmental protein, mrna processing, nuclear transport, mrna splicing, mrna transport
Biological sourceDROSOPHILA MELANOGASTER (FRUIT FLY)
More
Total number of polymer chains6
Total formula weight295628.18
Authors
Bono, F.,Cook, A.G.,Gruenwald, M.,Ebert, J.,Conti, E. (deposition date: 2009-12-23, release date: 2010-02-16, Last modification date: 2023-12-20)
Primary citationBono, F.,Cook, A.G.,Grunwald, M.,Ebert, J.,Conti, E.
Nuclear Import Mechanism of the Ejc Component Mago- Y14 Revealed by Structural Studies of Importin 13.
Mol.Cell, 37:211-, 2010
Cited by
PubMed Abstract: Mago and Y14 are core components of the exon junction complex (EJC), an assembly central to nonsense-mediated mRNA decay in humans and mRNA localization in flies. The Mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm, where it functions in translational regulation. The heterodimer is imported back into the nucleus by Importin 13 (Imp13), a member of the karyopherin-beta family of transport factors. We have elucidated the structural basis of the Mago-Y14 nuclear import cycle. The 3.35 A structure of the Drosophila Imp13-Mago-Y14 complex shows that Imp13 forms a ring-like molecule, reminiscent of Crm1, and encircles the Mago-Y14 cargo with a conserved interaction surface. The 2.8 A structure of human Imp13 bound to RanGTP reveals how Mago-Y14 is released in the nucleus by a steric hindrance mechanism. Comparison of the two structures suggests how this unusual karyopherin might function in bidirectional nucleocytoplasmic transport.
PubMed: 20122403
DOI: 10.1016/J.MOLCEL.2010.01.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.35 Å)
Structure validation

226707

數據於2024-10-30公開中

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