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RSS FeedsConformational dynamics of the HIV Vif protein complex (Biophysical Journal)

 
 

23 march 2019 08:02:32

 
Conformational dynamics of the HIV Vif protein complex (Biophysical Journal)
 


HIV-1 viral infectivity factor (Vif) is an intrinsically disordered protein responsible for the ubiquitination of the APOBEC3 antiviral proteins. Vif folds when it binds the Cullin-RING E3 ligase CRL5 and the transcription cofactor CBF-?. A five-protein complex containing the substrate receptor (Vif, CBF-?, Elongin-B, Elongin-C) and Cullin5 (CUL5) has a published crystal structure, but dynamics of this VCBC-CUL5 complex have not been characterized. Here, we use Molecular Dynamics (MD) simulations and NMR to characterize the dynamics of the VCBC complex with and without CUL5 and an APOBEC3 protein bound.


 
81 viewsCategory: Biophysics
 
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