2026-10-11T15:32:12Z
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2026-10-01T17:28:36Z
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<p>Vpr recruits two UNG2 molecules to the DDB1-VprBP complex in the “ARM-up” state.</p>
Dianhong Wang (25157696)
Weijia Ding (554415)
Jingwei Xu (337549)
Ruofan Li (1568194)
Tamino Cairoli (25157699)
Qi Liu (33068)
Yiying Zhu (8675928)
Ye Xiang (522776)
Biophysics
Biochemistry
Cell Biology
Evolutionary Biology
Infectious Diseases
Plant Biology
Virology
various restriction factors
ring e3 ligase
larger tet2 fragment
findings could facilitate
diverse substrate recruitment
vprbp could enable
vprbp adopt either
xlink "> hiv
two &# 8220
recruits diverse substrates
bound host factors
like domains adopt
diverse vpr
host cul4
&# 8220
vprbp mediates
vprbp dimerization
receptor vprbp
&# 8221
structures highlight
structural basis
results pinpoint
molecular architecture
may assist
lish domain
key protein
guided development
divergent stoichiometries
directly interact
different vpr
conformational dynamics
accommodating vpr
1 vpr
1 hijacks
<p><b>(A)</b> Overall architecture of the DDB1-VprBP-Vpr-UNG2 quaternary complex. The structure is shown as ribbons. The domains are color-coded according to the scheme shown at the top. <b>(B)</b> Interactions among WD40 domain, Vpr, and UNG2. The WD40 domain is shown as a semi-transparent surface overlaid with ribbons. Vpr (dark green) and UNG2 (pink) are shown in ribbon representation. The zoomed-in views highlight the electrostatic and hydrophobic interactions between the WD40 domain and Vpr, as well as the hydrophobic interactions between Vpr and UNG2. Key residues involved in these interactions are labeled and represented as sticks.</p>
2026-10-01T17:28:02Z
Image
Figure
10.1371/journal.ppat.1014610.g004
https://figshare.com/articles/figure/_p_Vpr_recruits_two_UNG2_molecules_to_the_DDB1-VprBP_complex_in_the_ARM-up_state_p_/34047935
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