The SCF ubiquitin ligase: an extended look

Mol Cell. 2002 May;9(5):923-5. doi: 10.1016/s1097-2765(02)00538-5.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Cell Cycle Proteins / metabolism
  • Crystallography, X-Ray
  • Cullin Proteins*
  • Humans
  • Models, Molecular
  • Peptide Synthases / chemistry
  • Peptide Synthases / physiology*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Quaternary
  • S-Phase Kinase-Associated Proteins
  • SKP Cullin F-Box Protein Ligases
  • Structure-Activity Relationship

Substances

  • Cell Cycle Proteins
  • Cullin 1
  • Cullin Proteins
  • S-Phase Kinase-Associated Proteins
  • SKP Cullin F-Box Protein Ligases
  • Peptide Synthases