Nature Communications (Jan 2017)

An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase

  • Veronika Csizmok,
  • Stephen Orlicky,
  • Jing Cheng,
  • Jianhui Song,
  • Alaji Bah,
  • Neda Delgoshaie,
  • Hong Lin,
  • Tanja Mittag,
  • Frank Sicheri,
  • Hue Sun Chan,
  • Mike Tyers,
  • Julie D. Forman-Kay

DOI
https://doi.org/10.1038/ncomms13943
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 14

Abstract

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The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.