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oai:figshare.com:article/34047893 2026-10-01T17:28:20Z category_1 category_4 category_12 category_24 category_132 category_133 category_134 portal_5 item_type_1 month_year_10_2026

<p>Structural basis of the Vpr-mediated UNG2 recruitment.</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)</b> Comparison of the domain organizations in (<b>A</b>) the crystal structure (PDB ID: 5jk7) and (<b>B</b>) cryo-EM structure of DDB1-VprBP-Vpr-UNG2 complex. UNG2, VprBP-WD40, and DDB1-BPC are colored pink, blue, and cyan, respectively.</p> <p>(TIF)</p> 2026-10-01T17:28:02Z Image Figure 10.1371/journal.ppat.1014610.s013 https://figshare.com/articles/figure/_p_Structural_basis_of_the_Vpr-mediated_UNG2_recruitment_p_/34047893 CC BY 4.0