
pmid: 12553901
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.
Binding Sites, SKP Cullin F-Box Protein Ligases, Saccharomyces cerevisiae Proteins, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, F-Box Proteins, Ubiquitin-Protein Ligases, Cell Cycle Proteins, Protein Structure, Tertiary, Substrate Specificity, Structure-Activity Relationship, Cyclin E, Peptide Synthases, Phosphorylation, Ubiquitins, Protein Binding
Binding Sites, SKP Cullin F-Box Protein Ligases, Saccharomyces cerevisiae Proteins, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, F-Box Proteins, Ubiquitin-Protein Ligases, Cell Cycle Proteins, Protein Structure, Tertiary, Substrate Specificity, Structure-Activity Relationship, Cyclin E, Peptide Synthases, Phosphorylation, Ubiquitins, Protein Binding
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