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PDBsum entry 2xb2
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390 a.a.
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143 a.a.
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89 a.a.
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15 a.a.
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57 a.a.
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17 a.a.
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References listed in PDB file
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Key reference
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Title
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Insights into the recruitment of the nmd machinery from the crystal structure of a core ejc-Upf3b complex.
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Authors
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G.Buchwald,
J.Ebert,
C.Basquin,
J.Sauliere,
U.Jayachandran,
F.Bono,
H.Le hir,
E.Conti.
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Ref.
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Proc Natl Acad Sci U S A, 2010,
107,
10050-10055.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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In mammals, Up-frameshift proteins (UPFs) form a surveillance complex that
interacts with the exon junction complex (EJC) to elicit nonsense-mediated mRNA
decay (NMD). UPF3b is the component of the surveillance complex that bridges the
interaction with the EJC. Here, we report the 3.4 A resolution crystal structure
of a minimal UPF3b-EJC assembly, consisting of the interacting domains of five
proteins (UPF3b, MAGO, Y14, eIF4AIII, and Barentsz) together with RNA and
adenylyl-imidodiphosphate. Human UPF3b binds with the C-terminal domain
stretched over a composite surface formed by eIF4AIII, MAGO, and Y14. Residues
that affect NMD when mutated are found at the core interacting surfaces, whereas
differences between UPF3b and UPF3a map at peripheral interacting residues.
Comparison with the binding mode of the protein PYM underscores how a common
molecular surface of MAGO and Y14 recognizes different proteins acting at
different times in the same pathway. The binding mode to eIF4AIII identifies a
surface hot spot that is used by different DEAD-box proteins to recruit their
regulators.
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