BibTex format

author = {Lu, Z and Bergeron, JRC and Atkinson, RA and Schaller, T and Veselkov, DA and Oregioni, A and Yang, Y and Matthews, SJ and Malim, MH and Sanderson, MR},
doi = {10.1098/rsob.130100},
journal = {Open Biology},
pages = {1--11},
title = {Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction},
url = {},
volume = {3},
year = {2013}

RIS format (EndNote, RefMan)

AB - The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.
AU - Lu,Z
AU - Bergeron,JRC
AU - Atkinson,RA
AU - Schaller,T
AU - Veselkov,DA
AU - Oregioni,A
AU - Yang,Y
AU - Matthews,SJ
AU - Malim,MH
AU - Sanderson,MR
DO - 10.1098/rsob.130100
EP - 11
PY - 2013///
SN - 2046-2441
SP - 1
TI - Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction
T2 - Open Biology
UR -
UR -
UR -
UR -
VL - 3
ER -