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PDBsum entry 2anr
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RNA-binding protein/RNA
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PDB id
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2anr
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References listed in PDB file
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Key reference
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Title
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Protein-Rna and protein-Protein recognition by dual kh1/2 domains of the neuronal splicing factor nova-1.
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Authors
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M.Teplova,
L.Malinina,
J.C.Darnell,
J.Song,
M.Lu,
R.Abagyan,
K.Musunuru,
A.Teplov,
S.K.Burley,
R.B.Darnell,
D.J.Patel.
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Ref.
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Structure, 2011,
19,
930-944.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Nova onconeural antigens are neuron-specific RNA-binding proteins implicated in
paraneoplastic opsoclonus-myoclonus-ataxia (POMA) syndrome. Nova harbors three
K-homology (KH) motifs implicated in alternate splicing regulation of genes
involved in inhibitory synaptic transmission. We report the crystal structure of
the first two KH domains (KH1/2) of Nova-1 bound to an in vitro selected RNA
hairpin, containing a UCAG-UCAC high-affinity binding site. Sequence-specific
intermolecular contacts in the complex involve KH1 and the second UCAC repeat,
with the RNA scaffold buttressed by interactions between repeats. Whereas the
canonical RNA-binding surface of KH2 in the above complex engages in
protein-protein interactions in the crystalline state, the individual KH2 domain
can sequence-specifically target the UCAC RNA element in solution. The observed
antiparallel alignment of KH1 and KH2 domains in the crystal structure of the
complex generates a scaffold that could facilitate target pre-mRNA looping on
Nova binding, thereby potentially explaining Nova's functional role in splicing
regulation.
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