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        <datestamp>2026-10-01T17:28:35Z</datestamp>
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          <dc:title>&lt;p&gt;The WD40 domain of VprBP binds DDB1, which exhibits a dynamic BPB domain.&lt;/p&gt;</dc:title>
          <dc:creator>Dianhong Wang (25157696)</dc:creator>
          <dc:creator>Weijia Ding (554415)</dc:creator>
          <dc:creator>Jingwei Xu (337549)</dc:creator>
          <dc:creator>Ruofan Li (1568194)</dc:creator>
          <dc:creator>Tamino Cairoli (25157699)</dc:creator>
          <dc:creator>Qi Liu (33068)</dc:creator>
          <dc:creator>Yiying Zhu (8675928)</dc:creator>
          <dc:creator>Ye Xiang (522776)</dc:creator>
          <dc:subject>Biophysics</dc:subject>
          <dc:subject>Biochemistry</dc:subject>
          <dc:subject>Cell Biology</dc:subject>
          <dc:subject>Evolutionary Biology</dc:subject>
          <dc:subject>Infectious Diseases</dc:subject>
          <dc:subject>Plant Biology</dc:subject>
          <dc:subject>Virology</dc:subject>
          <dc:subject>various restriction factors</dc:subject>
          <dc:subject>ring e3 ligase</dc:subject>
          <dc:subject>larger tet2 fragment</dc:subject>
          <dc:subject>findings could facilitate</dc:subject>
          <dc:subject>diverse substrate recruitment</dc:subject>
          <dc:subject>vprbp could enable</dc:subject>
          <dc:subject>vprbp adopt either</dc:subject>
          <dc:subject>xlink "&gt; hiv</dc:subject>
          <dc:subject>two &amp;# 8220</dc:subject>
          <dc:subject>recruits diverse substrates</dc:subject>
          <dc:subject>bound host factors</dc:subject>
          <dc:subject>like domains adopt</dc:subject>
          <dc:subject>diverse vpr</dc:subject>
          <dc:subject>host cul4</dc:subject>
          <dc:subject>&amp;# 8220</dc:subject>
          <dc:subject>vprbp mediates</dc:subject>
          <dc:subject>vprbp dimerization</dc:subject>
          <dc:subject>receptor vprbp</dc:subject>
          <dc:subject>&amp;# 8221</dc:subject>
          <dc:subject>structures highlight</dc:subject>
          <dc:subject>structural basis</dc:subject>
          <dc:subject>results pinpoint</dc:subject>
          <dc:subject>molecular architecture</dc:subject>
          <dc:subject>may assist</dc:subject>
          <dc:subject>lish domain</dc:subject>
          <dc:subject>key protein</dc:subject>
          <dc:subject>guided development</dc:subject>
          <dc:subject>divergent stoichiometries</dc:subject>
          <dc:subject>directly interact</dc:subject>
          <dc:subject>different vpr</dc:subject>
          <dc:subject>conformational dynamics</dc:subject>
          <dc:subject>accommodating vpr</dc:subject>
          <dc:subject>1 vpr</dc:subject>
          <dc:subject>1 hijacks</dc:subject>
          <dc:description>&lt;p&gt;&lt;b&gt;(A)&lt;/b&gt; Interactions between VprBP and DDB1. The DDB1 BPA and BPC domains are shown in surface representation and colored by electrostatic potential (red, negative; white, neutral; blue, positive). The H-box of the VprBP WD40 domain (green) and the linker between LisH domain and WD40 domain (yellow) are shown as ribbons. The detailed contact interfaces are zoomed in to highlight key residues involved in the interactions. &lt;b&gt;(B)&lt;/b&gt; Interactions between the VprBP ARM-like and DDB1 BPC domains. The ARM-like, LisH, and BPC domains are colored yellow, orange, and cyan, respectively. The zoomed-in views highlight the interfacial residues, which are labeled and shown as sticks. &lt;b&gt;(C)&lt;/b&gt; Conformational flexibility of the DDB1 BPB domain. Left, overall structure of DDB1 (BPA, pink, BPB, green, BPC, cyan) in the DDB1-VprBP complex. Right, ribbon diagrams showing the dynamic conformations of the DDB1 BPB domain (green). The tilt angles represent the deviation of the BPB domain pseudo-sevenfold axis relative to the z axis. The cut-in plane, anchored at the centroid of the BPB domain, was generated with the first two eigenvectors of the domain. Red arrows indicate the direction of the pseudo-sevenfold axis. The ribbons localized to one side of the plane, which are involved in CUL4A recruitment, are colored light green.&lt;/p&gt;</dc:description>
          <dc:date>2026-10-01T17:28:02Z</dc:date>
          <dc:type>Image</dc:type>
          <dc:type>Figure</dc:type>
          <dc:identifier>10.1371/journal.ppat.1014610.g003</dc:identifier>
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          <dc:rights>CC BY 4.0</dc:rights>
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