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<p>Comparison of “ARM-up” and “ARM-down” states and WD40 domain positioning in VprBP.</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>Structural comparison of the “ARM-up” and “ARM-down” VprBP states. Ribbon diagram showing the superimposed “ARM-up” and “ARM-down” VprBP structures. Structures were aligned using the LisH and WD40 domains as a fixed reference. The “up” ARM-like domain and “down” ARM-like domain are colored yellow and cyan, respectively. The hinges connecting the ARM-like domain and LisH domain are highlighted in red (for the “up” state) and blue (for the “down” state), respectively.</p> <p>(TIF)</p>
2026-10-01T17:28:02Z
Image
Figure
10.1371/journal.ppat.1014610.s010
https://figshare.com/articles/figure/_p_Comparison_of_ARM-up_and_ARM-down_states_and_WD40_domain_positioning_in_VprBP_p_/34047884
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