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Conformational flexibility and rotation of the RING domain in activation of cullin–RING ligases

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The RING protein RBX-1 is implicated in both NEDDylation and ubiquitylation reactions. In this issue, new structural analysis reveals how conformational flexibility of the RBX-1 linker allows for a marked reorientation of the CUL1–RBX1 complex to facilitate transfer of NEDD8 or ubiquitin by closing the gap between the E2 catalytic site and the substrate.

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Figure 1: RBX1-mediated NEDDylation of CUL1 is facilitated by substantial rotation of the RBX1 RING domain.

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Authors and Affiliations

  1. Simin Rahighi is at the Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Japan.,

    Simin Rahighi

  2. Ivan Dikic is at the Frankfurt Institute for Molecular Life Sciences, Institute of Biochemistry 2, Goethe University School of Medicine, Frankfurt, Germany.,

    Ivan Dikic

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  1. Simin Rahighi
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  2. Ivan Dikic
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Correspondence to Ivan Dikic.

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Rahighi, S., Dikic, I. Conformational flexibility and rotation of the RING domain in activation of cullin–RING ligases. Nat Struct Mol Biol 18, 863–865 (2011). https://doi.org/10.1038/nsmb.2117

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