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Ubiquitinating a Phosphorylated Cdk Inhibitor on the Blades of the Cdc4 β-Propeller
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Ubiquitinating a Phosphorylated Cdk Inhibitor on the Blades of the Cdc4 β-Propeller

Peter K. Jackson and Peter Lawrence Jackson
Cell, Vol.112(2), pp.142-144
24/01/2003
PMID: 12553901

Abstract

Substrate binding by the SCF Cdc4 ubiquitin ligase is regulated by phosphorylation. In this issue of Cell, Orlicky et al. describe the crystal structure of the Cdc4 subunit bound to a high-affinity substrate phosphopeptide. This structure provides insights into the binding interaction and how a precise mechanism involving multiple regulatory phosphorylations may be mediated by a single binding site.
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https://doi.org/10.1016/S0092-8674(03)00041-2View
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