a3g

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RT A3G NC NC Nucleic Acid A3G Roadblock Mechanism for Deaminase- Independent Inhibition of HIV-1 Reverse Transcription by A3G Iwatani et al. Nucleic Acids Res. 35:7096 (2007) Unlike A3G, RT has poor binding affinity to single-stranded nucleic acids. Thus, RT cannot readily displace A3G once it is bound to the single-stranded RNA or DNA template and RT-catalyzed DNA elongation is blocked. NC binding to nucleic acids exhibits a high on-off rate and NC function is not affected by A3G. A3G, APOBEC3G RT, reverse transcri ptase NC, nucleocapsid pro tein

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Roadblock Mechanism for Deaminase-Independent Inhibition of HIV-1 Reverse Transcription by A3G. A3G. NC. RT. A3G. NC. Nucleic Acid. - Unlike A3G, RT has poor binding affinity to single-stranded nucleic acids. Thus, RT cannot readily displace A3G once it is bound to the single-stranded - PowerPoint PPT Presentation

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Page 1: A3G

RTA3G

NC

NCNucleic Acid

A3G

Roadblock Mechanism for Deaminase-Independent Inhibition of HIV-1 Reverse

Transcription by A3G

Iwatani et al. Nucleic Acids Res. 35:7096 (2007)

- Unlike A3G, RT has poor binding affinity to single-stranded nucleic acids. Thus, RT cannot readily displace A3G once it is bound to the single-stranded RNA or DNA template and RT-catalyzed DNA elongation is blocked. - NC binding to nucleic acids exhibits a high on-off rate and NC function is not affected by A3G.

A3G, APOBEC3G RT, reverse transcriptase NC, nucleocapsid protein