Tat
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tat
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The C-terminal 34 residues (1329-1362) of BRD4 are crucial for interaction with P-TEFb. Overexpression of the BRD4 P-TEFb-interacting domain disrupts the interaction between HIV-1 Tat and P-TEFb |
PubMed
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tat
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HIV-1 Tat directly interacts with elongin B as demonstrated by Tat-affinity column purification |
PubMed
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Vif
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vif
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HIV-1 complexes with TCEB2 (ELOB) |
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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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, 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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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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HIV-1 Vif mutants W5S, W21S, W38S, W89S, F112S, and F115S have a reduced ability to interact with CBF-beta, but these Vif hydrophobic residue mutations still interact with EloB |
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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The PPLP motif (residues 161-164) of HIV-1 Vif binds to the C-terminal region (residues 101-118) of ElonginB |
PubMed
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vif
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Overexpression of EloB increases HIV-1 Vif stability in cells. The N-terminal residues 9-14 of EloB are involved in EloB-mediated stability of Vif |
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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The interaction between the HIV-1 Vif PPLP motif (residues 161-164) and the 34-amino-acid C-terminal tail (residues 85-118) of EloB plays a role in promoting recruitment of CBF-beta to the Vif-Cul5 E3 complex |
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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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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