| pubmed-article:10748161 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C0028606 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C0085431 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10748161 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
| pubmed-article:10748161 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:10748161 | pubmed:dateCreated | 2000-6-30 | lld:pubmed |
| pubmed-article:10748161 | pubmed:abstractText | Cys(38) and Cys(280) of p66/p51 human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) can be converted to Ser without affecting enzyme function. We have exploited this feature to construct and purify "monocysteine" RT derivatives for site-specific modification with the photoactivable cross-linking agent, p-azidophenacyl bromide. Acylation of a unique cysteine residue introduced at the extreme C terminus of the p66 subunit (C(561)) with an azidophenacyl group allowed us to probe contacts between residues C-terminal to alpha-helix E' of the RNase H domain and structurally divergent nucleic acid duplexes. In a binary complex of RT and template-primer, we demonstrate efficient cross-linking to primer nucleotides -21 to -24/-25, and template nucleotides -18 to -21. Cross-linking specificity was confirmed by an analogous evaluation following limited primer extension, where the profile is displaced by the register of DNA synthesis. Finally, contact with a DNA primer hybridized to an isogenic RNA or DNA template indicates subtle alterations in cross-linking specificity, suggesting differences in nucleic acid geometry between duplex DNA and RNA/DNA hybrids at the RNase H domain. These data exemplify how site-specific acylation of HIV-1 RT can be used to provide high resolution structural data to complement crystallographic studies. | lld:pubmed |
| pubmed-article:10748161 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10748161 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10748161 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10748161 | pubmed:month | May | lld:pubmed |
| pubmed-article:10748161 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10748161 | pubmed:author | pubmed-author:Sathyanarayan... | lld:pubmed |
| pubmed-article:10748161 | pubmed:author | pubmed-author:Le GriceS FSF | lld:pubmed |
| pubmed-article:10748161 | pubmed:author | pubmed-author:RauschJ WJW | lld:pubmed |
| pubmed-article:10748161 | pubmed:author | pubmed-author:BonkM EME | lld:pubmed |
| pubmed-article:10748161 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10748161 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:10748161 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10748161 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10748161 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10748161 | pubmed:pagination | 16015-22 | lld:pubmed |
| pubmed-article:10748161 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
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| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:meshHeading | pubmed-meshheading:10748161... | lld:pubmed |
| pubmed-article:10748161 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10748161 | pubmed:articleTitle | Probing contacts between the ribonuclease H domain of HIV-1 reverse transcriptase and nucleic acid by site-specific photocross-linking. | lld:pubmed |
| pubmed-article:10748161 | pubmed:affiliation | HIV Drug Resistance Program, Science Applications International Corporation, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, Maryland 21072, USA. | lld:pubmed |
| pubmed-article:10748161 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10748161 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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