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PDBsum entry 2ma9
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Viral protein/protein binding
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PDB id
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2ma9
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References listed in PDB file
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Key reference
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Title
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Insight into the HIV-1 vif socs-Box-Elonginbc interaction.
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Authors
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Z.Lu,
J.R.Bergeron,
R.A.Atkinson,
T.Schaller,
D.A.Veselkov,
A.Oregioni,
Y.Yang,
S.J.Matthews,
M.H.Malim,
M.R.Sanderson.
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Ref.
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Open Biol, 2013,
3,
130100.
[DOI no: ]
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PubMed id
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Abstract
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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.
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