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PDBsum entry 2u2f
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RNA binding protein
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PDB id
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2u2f
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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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Solution structures of the first and second RNA-Binding domains of human u2 small nuclear ribonucleoprotein particle auxiliary factor (u2af(65)).
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Authors
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T.Ito,
Y.Muto,
M.R.Green,
S.Yokoyama.
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Ref.
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EMBO J, 1999,
18,
4523-4534.
[DOI no: ]
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PubMed id
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Abstract
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The large subunit of the human U2 small nuclear ribonucleoprotein particle
auxiliary factor (hU2AF(65)) is an essential RNA-splicing factor required for
the recognition of the polypyrimidine tract immediately upstream of the 3'
splice site. In the present study, we determined the solution structures of two
hU2AF(65) fragments, corresponding to the first and second RNA-binding domains
(RBD1 and RBD2, respectively), by nuclear magnetic resonance spectroscopy. The
tertiary structure of RBD2 is similar to that of typical RNA-binding domains
with the beta1-alpha1-beta2-beta3-alpha2-beta4 topology. In contrast, the
hU2AF(65) RBD1 structure has unique features: (i) the alpha1 helix is elongated
by one turn toward the C-terminus; (ii) the loop between alpha1 and beta2 (the
alpha1/beta2 loop) is much longer and has a defined conformation; (iii) the
beta2 strand is (188)AVQIN(192), which was not predicted by sequence alignments;
and (iv) the beta2/beta3 loop is much shorter. Chemical shift perturbation
experiments showed that the U2AF-binding RNA fragments interact with the four
beta-strands of RBD2 whereas, in contrast, they interact with beta1, beta3 and
beta4, but not with beta2 or the alpha1/beta2 loop, of RBD1. The characteristic
alpha1-beta2 structure of the hU2AF(65) RBD1 may interact with other proteins,
such as UAP56.
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Figure 1.
Figure 1 A schematic diagram of the domain structure of
hU2AF^65. The RS domain refers to the arginine/serine-rich
domain, and RBD stands for an RNA-binding domain. The arrows
indicate the N- and C-terminal positions of the polypeptides
used in this study.
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Figure 8.
Figure 8 Possible base-binding positions of the hU2AF^65 RBD1
and RBD2. The amino acid residues that might stack with bases in
the first, second and third canonical base-binding sites are
shown, colored in magenta, green and cyan, respectively. On each
binding site, a schematic pyrimidine base and a N1–C1' bond
are presented.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
4523-4534)
copyright 1999.
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