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PDBsum entry 1qm9
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Ribonucleoprotein
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PDB id
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1qm9
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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 tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the rrm fold.
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Authors
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M.R.Conte,
T.Grüne,
J.Ghuman,
G.Kelly,
A.Ladas,
S.Matthews,
S.Curry.
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Ref.
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EMBO J, 2000,
19,
3132-3141.
[DOI no: ]
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PubMed id
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Abstract
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Polypyrimidine tract binding protein (PTB), an RNA binding protein containing
four RNA recognition motifs (RRMs), is involved in both pre-mRNA splicing and
translation initiation directed by picornaviral internal ribosome entry sites.
Sequence comparisons previously indicated that PTB is a non-canonical RRM
protein. The solution structure of a PTB fragment containing RRMs 3 and 4 shows
that the protein consists of two domains connected by a long, flexible linker.
The two domains tumble independently in solution, having no fixed relative
orientation. In addition to the betaalphabetabetaalphabeta topology, which is
characteristic of RRM domains, the C-terminal extension of PTB RRM-3
incorporates an unanticipated fifth beta-strand, which extends the RNA binding
surface. The long, disordered polypeptide connecting beta4 and beta5 in RRM-3 is
poised above the RNA binding surface and is likely to contribute to RNA
recognition. Mutational analyses show that both RRM-3 and RRM-4 contribute to
RNA binding specificity and that, despite its unusual sequence, PTB binds RNA in
a manner akin to that of other RRM proteins.
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Figure 3.
Figure 3 Ribbon diagrams for PTB-34 and Sex-lethal. (A)
Comparison of tandem domain structures of PTB and Sex-lethal.
The relative orientation of the two domains shown for PTB is
arbitrary, as is the structure of the inter-domain linker. The
structure of Sex-lethal was solved crystallographically in the
presence of bound RNA (Handa et al., 1999), which has been
omitted from the figure. (B) Comparison of RRM-3 and RRM-4
domains from PTB with RRM-1 of Sex-lethal. PTB RRM-3 contains an
additional strand (  5)
on one side of the RNA binding surface. Note that the
conformation shown for the 4–
5
loop is only one of many conformations that are consistent with
the data (see Figure 2).
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Figure 5.
Figure 5 Overview of protein and RNA constructs used in this
study. (A) Schematic depiction of PTB constructs; RRM domains
are indicated by shading. (B) Schematic diagram of the EMCV
IRES; domain 1 is boxed.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2000,
19,
3132-3141)
copyright 2000.
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Secondary reference #1
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Title
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Resonance assignment and topology of a 22kda c-Terminal fragment of the polypyriine tract binding protein containing two RNA binding domain
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Authors
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M.R.Conte,
T.Grune,
S.Curry,
S.Matthews.
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Ref.
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j biomol nmr, 1999,
14,
383.
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