The SCF ubiquitin ligase: an extended look.
The SCF E3 ubiquitin ligases select specific proteins for ubiquitination (and typically destruction) by coupling variable adaptor (F box) proteins that bind protein substrates to a conserved catalytic engine containing a cullin, Cul1, and the Rbx1/Roc1 RING finger protein. A new crystal structure of the SCF(Skp2) ubiquitin ligase shows the molecular organization of this complex and raises important questions as to how substrate ubiquitination is accomplished.
Jackson
Peter K
PK
Stanford University School of Medicine, Department of Pathology, 300 Pasteur Drive, Palo Alto, CA 94305, USA.
Eldridge
Adam G
AG
D018797:Cell Cycle Proteins / Q000378:metabolism; D018360:Crystallography, X-Ray; D044842:Cullin Proteins; D006801:Humans; D008958:Models, Molecular; D010453:Peptide Synthases / Q000737:chemistry / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D044786:S-Phase Kinase-Associated Proteins; D044843:SKP Cullin F-Box Protein Ligases; D013329:Structure-Activity Relationship
D018797:Cell Cycle Proteins; C100318:Cullin 1; D044842:Cullin Proteins; D044786:S-Phase Kinase-Associated Proteins; D044843:SKP Cullin F-Box Protein Ligases; D010453:Peptide Synthases