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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1991-4-25
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pubmed:abstractText |
An RNA recognition motif (RRM) of approximately 80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human U1 small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-1696729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-183204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-1976507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2140872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2197994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2207079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2390971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2467746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2470643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2479579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2479982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2531658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2547076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2673535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2685324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2830282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-2962859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3047011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3047743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3047872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3072706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3144435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3295261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3309338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3313012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3463963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3537727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-3542034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-6365163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-7020376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-7365797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1826055-845952
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2495-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1826055-Amino Acid Sequence,
pubmed-meshheading:1826055-Binding Sites,
pubmed-meshheading:1826055-Escherichia coli,
pubmed-meshheading:1826055-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1826055-Models, Molecular,
pubmed-meshheading:1826055-Molecular Sequence Data,
pubmed-meshheading:1826055-Protein Conformation,
pubmed-meshheading:1826055-RNA, Small Nuclear,
pubmed-meshheading:1826055-Recombinant Proteins,
pubmed-meshheading:1826055-Ribonucleoproteins,
pubmed-meshheading:1826055-Ribonucleoproteins, Small Nuclear,
pubmed-meshheading:1826055-Ribosomal Proteins,
pubmed-meshheading:1826055-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
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pubmed:affiliation |
Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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