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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1991-2-20
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pubmed:abstractText |
Eukaryotic nuclear RNA binding proteins share a common sequence motif thought to be implicated in RNA binding. One of the two domains present in A1 hnRNP protein, has been modelled by homology in order to make a prediction of the main features of the RNA binding site. Acylphosphatase (EC 3.6.1.7) was selected as template for the modeling experiment. The predicted RNA binding site is a beta-sheet containing the two RNP consensus sequences as well as lysines and arginines conserved among the family.
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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 |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
272-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2176620-Acid Anhydride Hydrolases,
pubmed-meshheading:2176620-Amino Acid Sequence,
pubmed-meshheading:2176620-Circular Dichroism,
pubmed-meshheading:2176620-Heterogeneous-Nuclear Ribonucleoprotein Group A-B,
pubmed-meshheading:2176620-Heterogeneous-Nuclear Ribonucleoproteins,
pubmed-meshheading:2176620-Models, Molecular,
pubmed-meshheading:2176620-Molecular Sequence Data,
pubmed-meshheading:2176620-Phosphoric Monoester Hydrolases,
pubmed-meshheading:2176620-Protein Conformation,
pubmed-meshheading:2176620-Ribonucleoproteins
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pubmed:year |
1990
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pubmed:articleTitle |
Modeling by homology of RNA binding domain in A1 hnRNP protein.
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pubmed:affiliation |
Instituto di Scienze Biologiche, Università di Verona, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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