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oai:figshare.com:article/34047887 2026-10-01T17:28:17Z 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 architecture and orientation of the VprBP WD40 domain.</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> Ribbon diagrams highlighting the H-box tail and β-propeller architecture of the WD40 domain. The β-propeller is constituted by seven WD40 repeats, each consisting of an antiparallel β-sheet formed by four short β-strands. <b>(B)</b> Spatial orientation of the WD40 domain. Ribbon diagram shows the spatial position of the WD40 domains (blue) relative to other domains of VprBP (gray). The red dashed lines indicate the pseudo-sevenfold axis of the WD40 domain.</p> <p>(TIF)</p> 2026-10-01T17:28:02Z Image Figure 10.1371/journal.ppat.1014610.s011 https://figshare.com/articles/figure/_p_Structural_architecture_and_orientation_of_the_VprBP_WD40_domain_p_/34047887 CC BY 4.0