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      The assembly of Vif ubiquitin E3 ligase for APOBEC3 degradation

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      https://www.riss.kr/link?id=A103902266

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      다국어 초록 (Multilingual Abstract)

      APOBEC3G is a cellular antiviral protein thatrestricts retroviral infection. In non-permissive cellsinfected by Vif-deficient HIV-1, the protein mediates thehypermutation of viral DNA through the enzymatic activityof cytidine deaminase. To counteract ...

      APOBEC3G is a cellular antiviral protein thatrestricts retroviral infection. In non-permissive cellsinfected by Vif-deficient HIV-1, the protein mediates thehypermutation of viral DNA through the enzymatic activityof cytidine deaminase. To counteract the antiviral activityof APOBEC3G, an accessory protein of HIV-1, Vif, formsubiquitin E3 ligase through assembly with CUL5-RBX2,ELOB-ELOC and CBFb. Subsequently, Vif recruitsAPOBEC3G to the complex as a substrate adaptor ofubiquitin E3 ligase and induces poly-ubiquitination ofAPOBEC3G for its proteasomal degradation (Fig. 1). Thisreview briefly summarizes current understanding of protein–protein interaction between Vif and host factorsrequired for APOBEC3 degradation, based on high resolutionstructures of APOBEC3 proteins and Vif-CUL5NTD-ELOBC-CBFb complex.

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      참고문헌 (Reference)

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      2 Paul, I., "Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions" 103 : 18475-18480, 2006

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