Ubiquitinating a phosphorylated Cdk inhibitor on the blades of the Cdc4 beta-propeller.
Substrate binding by the SCFCdc4 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.
Jackson
Peter K
PK
Programs in Chemical Biology and Cancer Biology and Department of Pathology, Stanford University School of Medicine, 300 Pasteur Drive, Stanford, CA 94305, USA.
D001665:Binding Sites; D018797:Cell Cycle Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D019927:Cyclin E / Q000737:chemistry* / Q000378:metabolism*; D044783:F-Box Proteins; D046911:Macromolecular Substances; D010453:Peptide Synthases / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D044843:SKP Cullin F-Box Protein Ligases; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins / Q000378:metabolism*
D018797:Cell Cycle Proteins; D019927:Cyclin E; D044783:F-Box Proteins; D046911:Macromolecular Substances; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; D044843:SKP Cullin F-Box Protein Ligases; D044767:Ubiquitin-Protein Ligases; D010453:Peptide Synthases