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A3G

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

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A3G

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

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