Abstract
HIV-1 viral infectivity factor (Vif) is a disordered protein that is responsible for ubiquitination and degradation of APOBEC antiviral proteins during HIV infection. Vif hijacks the Cullin-RING E3 ligase complex responsible for the ubiquitination process in healthy cells. Vif binds to core binding factor β (CBFβ), ELONGIN B (ELOB) and ELONGIN C (ELOC) to form the VCBC complex, part of the larger Cullin-RING E3 ligase complex. Molecular dynamics (MD) simulations can be used to study the conformational dynamics and interactions between proteins in the VCBC complex.
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