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Vif
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vif
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HIV-1 complexes with TCEB1 (ELOC) |
PubMed
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vif
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HIV-1 Vif interacts with TCEB1 (Elongin C) as demonstrated by co-immunoprecipitation assay |
PubMed
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vif
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ASK1 inhibits the interaction of HIV-1 Vif with ELOB/C in a dose-dependent manner, whereas no significant change is observed in the binding of Vif with CUL5 or CBFbeta |
PubMed
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vif
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ASK1 markedly inhibits HIV-1 Vif-induced ubiquitination of APOBEC3G by a reduction in the Vif-ELOC interaction |
PubMed
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vif
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HIV-1 Vif, CBF-beta, CUL5, and ELOB/C form a complex that is required for Vif-mediated downregulation of A3G and A3F. CBF-beta regulates HIV-1 infectivity only in the presence of A3G |
PubMed
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vif
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An overall crystal structure indicates that the Vif-CBF-beta-CUL5-ELOB-ELOC complex has a U-shape architecture, including the two straight arms Vif-CBF-beta and CUL5 and the bent arm formation between ELOC and CUL5 and Vif interactions |
PubMed
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vif
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Mutations in HIV-1 Vif PPLP motif (amino acids 161-164) reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5 |
PubMed
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vif
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HIV-1 Vif (amino acids 144-149; SLQXLA motif) interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-Cullin-F-box (SCF)-like complex that allows Vif to interact with APOBEC3G and induce its ubiquitination and degradation |
PubMed
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vif
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NMR solution structure indicates that HIV-1 Vif residues L145, A149, and L150 and ELOC residues A99 and L103 are involved in the interaction between Vif and ELOC |
PubMed
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vif
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Mutagenesis analysis indicates that HIV-1 Vif residues T123, R127, L145, and A149 and ELOC residues A100, L101, and L104 are involved in the interaction between Vif and ELOC |
PubMed
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vif
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Simultaneous substitution of the three Vif-interacting residues L52, W53, and D55 and the two ELOC-interacting residues P41 and H48 in CUL5 impairs the ability of CUL5 to interact with the Vif-CBF-beta-ELOB-ELOC protein complex |
PubMed
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vif
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The absence of Vif-CBF-beta reduces the interaction between the CUL5 and the EloC-EloB complex, indicating that the former two proteins have a critical role in promoting assembly of the pentameric complex |
PubMed
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vif
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Amino acid residues Vif135-158 have the most binding to the Elongin BC complex and undergo a structural change in the presence of Elongin BC |
PubMed
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vif
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The solubility of HIV-1 Vif is significantly enhanced by co-expression of EloB, EloC, and CBF-beta in vitro |
PubMed
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vif
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The substitution of Leu64 or Ile66 with serine abolishes the ability of CBF-beta to interact with the Vif-EloB/EloC complex, while the substitution of Thr68 or Tyr69 with alanine has an intermediate effect on the interaction of CBF-beta with the complex |
PubMed
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vif
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The interaction of HIV-1 Vif with EloB/EloC complex is important for the binding of Vif to CBF-beta in cells. The Vif SOCS box mutant (SLQ to AAA) significantly disrupt its interaction with the EloB/EloC complex |
PubMed
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vif
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A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C |
PubMed
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vif
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CUL5/RBX2/ELOB/ELOC/Vif/CBF-beta complex catalyzes polyubiquitin chain formation on A3G in the presence of ubiquitin E2 UBE2R1 (CDC34) or UBCH5b (UBE2D2) |
PubMed
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vif
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HIV-1 Vif binding to ElonginC is negatively regulated by serine phosphorylation in the BC-box of the Vif SOCS-box motif, and mutating amino acid S144 in Vif prevents phosphorylation at this site, significantly impairing Vif function and viral replication |
PubMed
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