Source:http://linkedlifedata.com/resource/pubmed/id/11401293
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-6-12
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| pubmed:abstractText |
HIV-1 reverse transcriptase (HIV-1 RT) is a multifunctional enzyme responsible for converting viral RNA into preintegrative DNA during the early stages of viral infection. DNA polymerase and RNase H activities are required, and several conformationally distinct primer-templates must be accommodated by the enzyme during the process. Parameters of interaction between model substrates (ligands) and HIV-1 RT (wild type p66/p51 and the RNase H-deficient mutant p66(E478Q)/p51) (analytes) were estimated by surface plasmon resonance at 25 degrees C, pH 8.0. Binding of RT to the ligands is specific and can be analyzed using a conventional 1:1 binding algorithm. RNA-DNA hybrids with 5'-template overhangs of 6 and 12 nucleotides bind to RT approximately one order of magnitude stronger than the corresponding 36-mer with blunt ends due to slower dissociation. Immobilization of the latter through either the 5'-end of RNA or DNA strand does not change the equilibrium constant (K(D)) for wild-type RT but the values of kinetic constants of association and dissociation differ significantly. For the p66(E478Q)/p51 enzyme, orientation effects are notable even altering the K(D) value. Binding of the p66(E478Q)/p51 to any RNA-DNA hybrids is slightly stronger compared with wild type. Data can be interpreted in terms of the mechanism of reverse transcription.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Reverse Transcriptase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acid Heteroduplexes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0003-2697
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
291
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
198-206
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11401293-Algorithms,
pubmed-meshheading:11401293-Base Sequence,
pubmed-meshheading:11401293-Binding, Competitive,
pubmed-meshheading:11401293-Biotinylation,
pubmed-meshheading:11401293-DNA,
pubmed-meshheading:11401293-DNA Primers,
pubmed-meshheading:11401293-HIV Reverse Transcriptase,
pubmed-meshheading:11401293-HIV-1,
pubmed-meshheading:11401293-Kinetics,
pubmed-meshheading:11401293-Ligands,
pubmed-meshheading:11401293-Mutation,
pubmed-meshheading:11401293-Nucleic Acid Heteroduplexes,
pubmed-meshheading:11401293-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:11401293-Protein Binding,
pubmed-meshheading:11401293-RNA,
pubmed-meshheading:11401293-Substrate Specificity,
pubmed-meshheading:11401293-Surface Plasmon Resonance,
pubmed-meshheading:11401293-Templates, Genetic,
pubmed-meshheading:11401293-Thermodynamics
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| pubmed:year |
2001
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| pubmed:articleTitle |
HIV-1 reverse transcriptase interaction with model RNA-DNA duplexes.
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| pubmed:affiliation |
Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, NIH, Bethesda, Maryland 20892, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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