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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6505
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pubmed:dateCreated |
1994-12-30
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pubmed:abstractText |
The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined at 1.92 A resolution. The ten-nucleotide RNA loop binds to the surface of the beta-sheet as an open structure, and the AUUGCAC sequence of the loop interacts extensively with the conserved RNP1 and RNP2 motifs and the C-terminal extension of the RNP domain. These interactions include stacking of RNA bases with aromatic side chains of proteins and many direct and water-mediated hydrogen bonds. The structure reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
372
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
432-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7984237-Amino Acid Sequence,
pubmed-meshheading:7984237-Base Sequence,
pubmed-meshheading:7984237-Binding Sites,
pubmed-meshheading:7984237-Crystallography, X-Ray,
pubmed-meshheading:7984237-Hydrogen Bonding,
pubmed-meshheading:7984237-Models, Molecular,
pubmed-meshheading:7984237-Molecular Sequence Data,
pubmed-meshheading:7984237-Nucleic Acid Conformation,
pubmed-meshheading:7984237-Protein Structure, Secondary,
pubmed-meshheading:7984237-Protein Structure, Tertiary,
pubmed-meshheading:7984237-RNA, Small Nuclear,
pubmed-meshheading:7984237-RNA-Binding Proteins,
pubmed-meshheading:7984237-Ribonucleoprotein, U1 Small Nuclear,
pubmed-meshheading:7984237-Spliceosomes
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pubmed:year |
1994
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pubmed:articleTitle |
Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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