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PDBsum entry 2xc7
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RNA binding protein
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PDB id
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2xc7
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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 and RNA recognition by the snrna and snorna transport factor phax.
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Authors
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A.Mourão,
A.Varrot,
C.D.Mackereth,
S.Cusack,
M.Sattler.
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Ref.
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Rna, 2010,
16,
1205-1216.
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PubMed id
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Abstract
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Small nuclear and small nucleolar RNAs (snRNAs and snoRNAs) are critical
components of snRNPs and snoRNPs and play an essential role in the maturation
of, respectively, mRNAs and rRNAs within the nucleus of eukaryotic cells.
Complex and specific pathways exist for the assembly of snRNPs and snoRNPs,
involving, for instance, nucleocytoplasmic transport of snRNAs and intranuclear
transport between compartments of snoRNAs. The phosphorylated adaptor for
nuclear export (PHAX) is required for nuclear export of snRNAs in metazoans and
also involved in the intranuclear transport of snoRNAs to Cajal bodies. PHAX
contains a conserved single-stranded nucleic acid binding domain (RNA_GG_bind
domain) with no sequence homology with any other known RNA-binding module. Here,
we report NMR and X-ray crystallography studies that elucidate the structural
basis for RNA recognition by the PHAX RNA-binding domain (PHAX-RBD). The crystal
structure of the RNA_GG_bind domain from the parasite Cryptosporidium parvum (Cp
RBD) forms well-folded dimers in solution in the absence of any ligand. The
human PHAX-RBD is monomeric and only adopts a tertiary fold upon RNA binding.
The PHAX-RBD represents a novel helical fold and binds single-stranded RNA with
micromolar affinity without sequence specificity. RNA recognition by human
PHAX-RBD is consistent with mutational analysis that affects RNA binding and
PHAX-mediated nuclear export. Our data suggest that the PHAX-RBD mediates
auxiliary RNA contacts with the snRNA and snoRNA substrates that are required
for transport and/or substrate release.
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