@article{Lu:2013:10.1098/rsob.130100,
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 = {http://dx.doi.org/10.1098/rsob.130100},
volume = {3},
year = {2013}
}

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TY  - JOUR
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  - http://dx.doi.org/10.1098/rsob.130100
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000330307000001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://royalsocietypublishing.org/doi/10.1098/rsob.130100
UR  - http://hdl.handle.net/10044/1/77389
VL  - 3
ER  - 

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