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ABSTRACT: Background
Human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) forms stable ternary complexes in which RT is bound tightly at fixed positions on the primer-template (P/T). We have probed downstream interactions between RT and the template strand in the complex containing the incoming dNTP (+1 dNTP*RT*P/T complex) and in the complex containing the pyrophosphate analog, foscarnet (foscarnet*RT*P/T complex).Methods and results
UV-induced cross-linking between RT and the DNA template strand was most efficient when a bromodeoxyuridine residue was placed in the +2 position (the first template position downstream from the incoming dNTP). Furthermore, formation of the +1 dNTP*RT*P/T complex on a biotin-containing template inhibited binding of streptavidin when biot
SUBMITTER: Rutvisuttinunt W
PROVIDER: S-EPMC2570493 | biostudies-literature | 2008
REPOSITORIES: biostudies-literature