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rdf:type |
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lifeskim:mentions |
umls-concept:C0035687,
umls-concept:C0521390,
umls-concept:C0524637,
umls-concept:C0911154,
umls-concept:C1416568,
umls-concept:C1514562,
umls-concept:C1521761,
umls-concept:C1554184,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
7
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pubmed:dateCreated |
2011-7-11
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1878-4186
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pubmed:author |
pubmed-author:AbagyanRubenR,
pubmed-author:BurleyStephen KSK,
pubmed-author:DarnellJennifer CJC,
pubmed-author:DarnellRobert BRB,
pubmed-author:LuMinM,
pubmed-author:MalininaLucyL,
pubmed-author:MusunuruKiranK,
pubmed-author:PatelDinshaw JDJ,
pubmed-author:SongJikuiJ,
pubmed-author:TeplovAlexeiA,
pubmed-author:TeplovaMariannaM
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
13
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
930-44
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pubmed:dateRevised |
2011-11-7
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pubmed:meshHeading |
pubmed-meshheading:21742260-Alternative Splicing,
pubmed-meshheading:21742260-Amino Acid Sequence,
pubmed-meshheading:21742260-Antigens, Neoplasm,
pubmed-meshheading:21742260-Base Sequence,
pubmed-meshheading:21742260-Binding Sites,
pubmed-meshheading:21742260-Crystallization,
pubmed-meshheading:21742260-Crystallography, X-Ray,
pubmed-meshheading:21742260-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:21742260-Humans,
pubmed-meshheading:21742260-Magnetic Resonance Spectroscopy,
pubmed-meshheading:21742260-Models, Molecular,
pubmed-meshheading:21742260-Molecular Sequence Data,
pubmed-meshheading:21742260-Nerve Tissue Proteins,
pubmed-meshheading:21742260-Neurons,
pubmed-meshheading:21742260-Opsoclonus-Myoclonus Syndrome,
pubmed-meshheading:21742260-Protein Binding,
pubmed-meshheading:21742260-Protein Structure, Tertiary,
pubmed-meshheading:21742260-RNA, Small Interfering,
pubmed-meshheading:21742260-RNA Precursors,
pubmed-meshheading:21742260-RNA-Binding Proteins,
pubmed-meshheading:21742260-Sequence Homology, Amino Acid,
pubmed-meshheading:21742260-Solutions,
pubmed-meshheading:21742260-Synaptic Transmission,
pubmed-meshheading:21742260-Syndrome
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pubmed:year |
2011
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pubmed:articleTitle |
Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1.
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pubmed:affiliation |
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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