| pubmed-article:17400246 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0070895 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0332298 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0205431 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
| pubmed-article:17400246 | lifeskim:mentions | umls-concept:C0146894 | lld:lifeskim |
| pubmed-article:17400246 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17400246 | pubmed:dateCreated | 2007-4-30 | lld:pubmed |
| pubmed-article:17400246 | pubmed:abstractText | Binding of the next complementary dNTP by the binary complex containing HIV-1 reverse transcriptase (RT) and primer-template induces conformational changes that have been implicated in catalytic function of RT. We have used DNase I footprinting, gel electrophoretic mobility shift, and exonuclease protection assays to characterize the interactions between HIV-1 RT and chain-terminated primer-template in the absence and presence of various ligands. Distinguishable stable complexes were formed in the presence of foscarnet (an analog of pyrophosphate), the dNTP complementary to the first (+1) templating nucleotide or the dNTP complementary to the second (+2) templating nucleotide. The position of HIV-1 RT on the primer-template in each of these complexes is different. RT is located upstream in the foscarnet complex, relative to the +1 complex, and downstream in the +2 complex. These results suggest that HIV-1 RT can translocate along the primer-template in the absence of phosphodiester bond formation. The ability to form a specific foscarnet complex might explain the inhibitory properties of this compound. The ability to recognize the second templating nucleotide has implications for nucleotide misincorporation. | lld:pubmed |
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| pubmed-article:17400246 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17400246 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17400246 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17400246 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17400246 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17400246 | pubmed:month | May | lld:pubmed |
| pubmed-article:17400246 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:17400246 | pubmed:author | pubmed-author:MeyerPeter... | lld:pubmed |
| pubmed-article:17400246 | pubmed:author | pubmed-author:MatsuuraSuzan... | lld:pubmed |
| pubmed-article:17400246 | pubmed:author | pubmed-author:SoAntero GAG | lld:pubmed |
