{"id":3902,"date":"2017-01-20T14:50:00","date_gmt":"2017-01-20T14:50:00","guid":{"rendered":"https:\/\/sites.dundee.ac.uk\/alessio-ciulli\/?p=3902"},"modified":"2026-01-28T09:54:31","modified_gmt":"2026-01-28T09:54:31","slug":"first-crystal-structure-of-the-vhl-elobc-cul2-rbx1-multi-subunit-complex","status":"publish","type":"post","link":"https:\/\/sites.dundee.ac.uk\/alessio-ciulli\/2017\/01\/20\/first-crystal-structure-of-the-vhl-elobc-cul2-rbx1-multi-subunit-complex\/","title":{"rendered":"First crystal structure of the VHL-EloBC-Cul2-Rbx1 multi-subunit complex"},"content":{"rendered":"\n

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\"Graphical
Graphical Abstract<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 1. Crystal Structure of the CRL2VHL Complex<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 2. The CRL2VHL Complex Is Dynamic and Flexible<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 3. Rbx1 Presents a New Orientation<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 4. The Cul2-VBC Interface” title=”Figure 4. The Cul2-VBC Interface<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 5. Biophysical Characterization of the Interaction between VBC and Cul2<\/figcaption><\/figure>\n\n\n\n
\"Figure6.
Figure6. Residues in the EloC Hydrophobic Pocket Reveal Criticality for the Strong Binding Affinity of Cul2-VBC<\/figcaption><\/figure>\n\n\n\n
\"Figure
Figure 7. Swapping Residues and Selectivity for Cul2 or Cul5<\/figcaption><\/figure>\n<\/figure>\n","protected":false},"excerpt":{"rendered":"

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