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PDBsum entry 1o0p
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RNA binding protein
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PDB id
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1o0p
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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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Structural basis for the molecular recognition between human splicing factors u2af65 and sf1/mbbp.
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Authors
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P.Selenko,
G.Gregorovic,
R.Sprangers,
G.Stier,
Z.Rhani,
A.Krämer,
M.Sattler.
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Ref.
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Mol Cell, 2003,
11,
965-976.
[DOI no: ]
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PubMed id
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Abstract
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The essential splicing factors SF1 and U2AF play an important role in the
recognition of the pre-mRNA 3' splice site during early spliceosome assembly.
The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an
N-terminal peptide of SF1 reveals an extended negatively charged helix A and an
additional helix C. Helix C shields the potential RNA binding surface. SF1 binds
to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a
hydrophobic pocket between helices A and B in a way that strikingly resembles
part of the molecular interface in the U2AF heterodimer. This molecular
recognition establishes a paradigm for protein binding by a subfamily of
noncanonical RRMs.
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Figure 4.
Figure 4. Tryptophan Recognition by the U2AF^35 RRM and
U2AF^65-RRM3(A) Ribbon representation of the U2AF^35 RRM in
complex with the proline-rich region in the N terminus of
U2AF^65 (Kielkopf et al., 2001). Side chains involved in the
molecular interface are shown. Trp134, which is not conserved in
U2AF^65-RRM3, is labeled magenta.(B) Ribbon representation of
the U2AF^65-RRM3/SF1 complex. Side chains involved in tryptophan
coordination are shown.(C) Sequence alignment of noncanonical
RRMs with an extended and negatively charged helix A.
Conserved residues that mediate recognition of SF1 Trp22 and
U2AF^65 Trp92 by U2AF^65-RRM3 and the U2AF^35 RRM, respectively,
are shown in white on black. Trp134 in the U2AF^35 RRM is
colored magenta.(D) Domain organization of proteins that contain
noncanonical RRMs. The domain annotations are according to SMART
(Schultz et al., 1998). “R/S” is an arginine-serine-rich
region, “STY Kc” is a phoshokinase domain, and “Zn” are
zinc binding domains.
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Figure 6.
Figure 6. Structure and Topology of Complex E during
Spliceosome AssemblyFor a description, see the text. An
additional interaction between the R/S domain of U2AF^65 and the
BPS (Valcárcel et al., 1996) is not shown.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2003,
11,
965-976)
copyright 2003.
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