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PDBsum entry 1p27
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RNA binding protein
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PDB id
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1p27
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the y14-Magoh core of the exon junction complex.
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Authors
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C.K.Lau,
M.D.Diem,
G.Dreyfuss,
G.D.Van duyne.
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Ref.
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Curr Biol, 2003,
13,
933-941.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Figure 2. Structure of Human Magoh(A) Alignment of a
diverse subset of known Magoh sequences. The shaded regions
indicate ≥80% sequence identity. Secondary structure
assignments are shown above the alignments, and residues
contacting Y14 (< 3.8 Å) are marked with an asterisk. Hs,
human; Dm, D. melanogaster; Ce, C. elegans; At, A. thaliana; Sp,
S. pombe.(B) A ribbon diagram of Magoh as seen bound to Y14.(C)
σ[A]-weighted 2Fo-Fc electron density for the refined structure
at 2 Å resolution, contoured at 1.4 σ. The orientation of
the indicated β strands is the same as that shown in (B).The
molecular drawings in Figure 2, Figure 3, Figure 4, Figure 5 and
Figure 6 were prepared with PYMOL [46].
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Figure 3.
Figure 3. Sequence Conservation Mapped onto the Magoh
StructureLight-blue residues correspond to the shaded regions in
Figure 2A (≥80% identity), and dark-blue residues are less
conserved.(A) Same orientation as in Figures 2B and 2C.(B) View
from the opposite face, showing the concave surface formed by
the β sheet extension.
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The above figures are
reprinted
by permission from Cell Press:
Curr Biol
(2003,
13,
933-941)
copyright 2003.
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