pubmed-article:7547980 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7547980 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:7547980 | lifeskim:mentions | umls-concept:C0441833 | lld:lifeskim |
pubmed-article:7547980 | lifeskim:mentions | umls-concept:C1514661 | lld:lifeskim |
pubmed-article:7547980 | pubmed:issue | 38 | lld:pubmed |
pubmed-article:7547980 | pubmed:dateCreated | 1995-11-6 | lld:pubmed |
pubmed-article:7547980 | pubmed:abstractText | The role of the 2'-hydroxyl group in RNA--protein interaction has been investigated using MS2 coat protein and its hairpin RNA operator as a model system. Derivatives of the MS2 translational operator were prepared where individual riboses were replaced by deoxyribose and their binding affinities to MS2 coat protein were determined. Only 1 (U-5) out of 15 positions tested reduced protein affinity by 1.6 kcal/mol. A variety of other 2'-modifications were tested at this position to understand the role of this particular 2'-hydroxyl group. Normal binding of the U-NH2 variant and weaker binding of the U-O-methyl variant are consistent with the ability of these functional groups to provide a hydrogen bond donor. This is also supported by recent crystallographic data which indicate a possible interaction between the 2'-hydroxyl of U-5 and the carboxylate group of glutamate 63 [Valegård et al. (1994) Nature 371, 623-626]. Complementary experiments introducing riboses into a DNA hairpin confirm the putative protein contact, and also identify a requirement for riboses in the two upper base pairs of the hairpin. Several arguments suggest these riboses are required to maintain an A-form helix in this region of the binding site. A minimum requirement of four 2'-hydroxyl groups for wild-type coat protein binding has been determined, one of which is at the -5 position and other three in the upper stem in any combination.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:7547980 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7547980 | pubmed:language | eng | lld:pubmed |
pubmed-article:7547980 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7547980 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7547980 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7547980 | pubmed:month | Sep | lld:pubmed |
pubmed-article:7547980 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:7547980 | pubmed:author | pubmed-author:UhlenbeckO... | lld:pubmed |
pubmed-article:7547980 | pubmed:author | pubmed-author:BaidyaNN | lld:pubmed |
pubmed-article:7547980 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7547980 | pubmed:day | 26 | lld:pubmed |
pubmed-article:7547980 | pubmed:volume | 34 | lld:pubmed |
pubmed-article:7547980 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7547980 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7547980 | pubmed:pagination | 12363-8 | lld:pubmed |
pubmed-article:7547980 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:7547980 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7547980 | pubmed:articleTitle | The role of 2'-hydroxyl groups in an RNA-protein interaction. | lld:pubmed |
pubmed-article:7547980 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215, USA. | lld:pubmed |
pubmed-article:7547980 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7547980 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:7547980 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7547980 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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