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

Nature Structural & Molecular Biology volume 18, pages 863865 (2011) | Download Citation

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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Author information

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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Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Ivan Dikic.

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DOI

https://doi.org/10.1038/nsmb.2117

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