pubmed-article:10445883 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:10445883 | lifeskim:mentions | umls-concept:C0966504 | lld:lifeskim |
pubmed-article:10445883 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:10445883 | pubmed:dateCreated | 1999-8-30 | lld:pubmed |
pubmed-article:10445883 | pubmed:abstractText | A novel metal-binding site has been identified in the hammerhead ribozyme by 31P NMR. The metal-binding site is associated with the A13 phosphate in the catalytic core of the hammerhead ribozyme and is distinct from any previously identified metal-binding sites. 31P NMR spectroscopy was used to measure the metal-binding affinity for this site and leads to an apparent dissociation constant of 250-570 microM at 25 degrees C for binding of a single Mg2+ ion. The NMR data also show evidence of a structural change at this site upon metal binding and these results are compared with previous data on metal-induced structural changes in the core of the hammerhead ribozyme. These NMR data were combined with the X-ray structure of the hammerhead ribozyme (Pley HW, Flaherty KM, McKay DB. 1994. Nature 372:68-74) to model RNA ligands involved in binding the metal at this A13 site. In this model, the A13 metal-binding site is structurally similar to the previously identified A(g) metal-binding site and illustrates the symmetrical nature of the tandem G x A base pairs in domain 2 of the hammerhead ribozyme. These results demonstrate that 31P NMR represents an important method for both identification and characterization of metal-binding sites in nucleic acids. | lld:pubmed |
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pubmed-article:10445883 | pubmed:language | eng | lld:pubmed |
pubmed-article:10445883 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10445883 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10445883 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10445883 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10445883 | pubmed:issn | 1355-8382 | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:HansenM RMR | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:PardoKK | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:HansonPP | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:BelloyCC | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:SimorreJ PJP | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:BeigelmanLL | lld:pubmed |
pubmed-article:10445883 | pubmed:author | pubmed-author:MoklerVV | lld:pubmed |
pubmed-article:10445883 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10445883 | pubmed:volume | 5 | lld:pubmed |
pubmed-article:10445883 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10445883 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10445883 | pubmed:pagination | 1099-104 | lld:pubmed |
pubmed-article:10445883 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10445883 | pubmed:meshHeading | pubmed-meshheading:10445883... | lld:pubmed |
pubmed-article:10445883 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10445883 | pubmed:articleTitle | Identification and characterization of a novel high affinity metal-binding site in the hammerhead ribozyme. | lld:pubmed |
pubmed-article:10445883 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Colorado at Boulder, 80309-0215, USA. | lld:pubmed |
pubmed-article:10445883 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10445883 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10445883 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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