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rdf:type |
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lifeskim:mentions |
umls-concept:C0086418,
umls-concept:C0162797,
umls-concept:C0205199,
umls-concept:C1167167,
umls-concept:C1167622,
umls-concept:C1321560,
umls-concept:C1423492,
umls-concept:C1514562,
umls-concept:C1710360,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
5821
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pubmed:dateCreated |
2007-4-6
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pubmed:abstractText |
Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRPF31 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PRPF6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoprotein, U4-U6 Small...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/U4 small nuclear RNA
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
316
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-20
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:17412961-Amino Acid Motifs,
pubmed-meshheading:17412961-Amino Acid Sequence,
pubmed-meshheading:17412961-Amino Acid Substitution,
pubmed-meshheading:17412961-Carrier Proteins,
pubmed-meshheading:17412961-Eye Proteins,
pubmed-meshheading:17412961-Humans,
pubmed-meshheading:17412961-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:17412961-Models, Molecular,
pubmed-meshheading:17412961-Molecular Sequence Data,
pubmed-meshheading:17412961-Mutation,
pubmed-meshheading:17412961-Nucleic Acid Conformation,
pubmed-meshheading:17412961-Protein Binding,
pubmed-meshheading:17412961-Protein Conformation,
pubmed-meshheading:17412961-Protein Structure, Secondary,
pubmed-meshheading:17412961-Protein Structure, Tertiary,
pubmed-meshheading:17412961-RNA, Small Nuclear,
pubmed-meshheading:17412961-RNA-Binding Proteins,
pubmed-meshheading:17412961-Retinitis Pigmentosa,
pubmed-meshheading:17412961-Ribonucleoprotein, U4-U6 Small Nuclear,
pubmed-meshheading:17412961-Transcription Factors
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pubmed:year |
2007
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pubmed:articleTitle |
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
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pubmed:affiliation |
Abteilung Zelluläre Biochemie, Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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