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PDBsum entry 1jmt
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RNA binding protein
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PDB id
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1jmt
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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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A novel peptide recognition mode revealed by the X-Ray structure of a core u2af35/u2af65 heterodimer.
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Authors
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C.L.Kielkopf,
N.A.Rodionova,
M.R.Green,
S.K.Burley.
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Ref.
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Cell, 2001,
106,
595-605.
[DOI no: ]
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PubMed id
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Abstract
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U2 auxiliary factor (U2AF) is an essential splicing factor that recognizes the
3' splice site and recruits the U2 snRNP to the branch point. The X-ray
structure of the human core U2AF heterodimer, consisting of the U2AF35 central
domain and a proline-rich region of U2AF65, has been determined at 2.2 A
resolution. The structure reveals a novel protein-protein recognition strategy,
in which an atypical RNA recognition motif (RRM) of U2AF35 and the U2AF65
polyproline segment interact via reciprocal "tongue-in-groove"
tryptophan residues. Complementary biochemical experiments demonstrate that the
core U2AF heterodimer binds RNA, and that the interacting tryptophan side chains
are essential for U2AF dimerization. Atypical RRMs in other splicing factors may
serve as protein-protein interaction motifs elsewhere during spliceosome
assembly.
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Figure 1.
Figure 1. Structure of the U2AF^35/U2AF^65 Complex(A)
Stereoview of the U2AF^65 proline-rich loop enveloping U2AF^35
Trp134. Density modified, experimental electron density map for
residues Trp92p to Pro104p of U2AF^65 contoured at 1σ. The
U2AF^65 peptide is shown in pink, or color coded for atom type
(yellow, carbon; red, oxygen; and blue, nitrogen) and the
U2AF^35 domain is shown in light blue. Six disordered amino
acids linking α helix A with the RNP2 β strand 1 are
represented with a dashed line. The RNP motifs and α helices A
and B are labeled.(B) The U2AF complex viewed along the
cylindrical axis of α helix A. A schematic representation of
the reciprocal tryptophan binding sites is shown on the left.(C)
View of the binary complex perpendicular to the perspective of
(B).(D) U2AF^35 β sheet that forms the RNA binding surfaces of
canonical RRM-containing proteins
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Figure 3.
Figure 3. Reciprocal Tryptophan Recognition within the U2AF
HeterodimerStereodrawings of interactions with (A) U2AF^35
Trp134 and (B) U2AF^65 Trp92p
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
106,
595-605)
copyright 2001.
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