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PDBsum entry 2adc
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RNA binding protein/RNA
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PDB id
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2adc
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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 ptb bound to RNA: specific binding and implications for splicing regulation.
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Authors
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F.C.Oberstrass,
S.D.Auweter,
M.Erat,
Y.Hargous,
A.Henning,
P.Wenter,
L.Reymond,
B.Amir-Ahmady,
S.Pitsch,
D.L.Black,
F.H.Allain.
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Ref.
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Science, 2005,
309,
2054-2057.
[DOI no: ]
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PubMed id
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Abstract
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The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding
protein involved in multiple aspects of messenger RNA metabolism, including the
repression of alternative exons. We have determined the solution structures of
the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU
oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3
and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs.
Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts
within the same RNA. This leads to structural models for how PTB functions as an
alternative-splicing repressor.
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Figure 1.
Fig. 1. Overlay of the structural ensemble and view of the most
representative structure for each RBD of PTB in complex with
RNA. Overlay of the 20 lowest energy structures of PTB RBD1 (A,
top), RBD2 (B, top), RBD3 (C, top), and RBD4 (D, top) in complex
with CUCUCU, the protein backbone, and the RNA heavy atoms of
the bound nucleotides are shown. View of the most representative
structure of each RBD in complex with CUCUCU: RBD1 (A, bottom),
RBD2 (B, bottom), RBD3 (C, bottom) and RBD4 (D, bottom).
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Figure 3.
Fig. 3. PTB RBD3 and RBD4 interdomain interactions. (A) Overlay
of the 20 lowest energy structures of PTB RBD34 in complex with
CUCUCU. RBD3 is in blue, RBD4 in green, the interdomain linker
in red, and the RNA in yellow. (B) View of the most
representative structure. The side chains contributing to the
interdomain interaction are shown by black sticks and by black
dots representing their surfaces.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2005,
309,
2054-2057)
copyright 2005.
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