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Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade.

The E6AP ubiquitin-protein ligase (E3) mediates the human papillomavirus-induced degradation of the p53 tumor suppressor in cervical cancer and is mutated in Angelman syndrome, a neurological disorder. The crystal structure of the catalytic hect domain of E6AP reveals a bilobal structure with a broad catalytic cleft at the junction of the two lobes. The cleft consists of conserved residues whose mutation interferes with ubiquitin-thioester bond formation and is the site of Angelman syndrome mutations. The crystal structure of the E6AP hect domain bound to the UbcH7 ubiquitin-conjugating enzyme (E2) reveals the determinants of E2-E3 specificity and provides insights into the transfer of ubiquitin from the E2 to the E3.

Pubmed ID: 10558980


  • Huang L
  • Kinnucan E
  • Wang G
  • Beaudenon S
  • Howley PM
  • Huibregtse JM
  • Pavletich NP


Science (New York, N.Y.)

Publication Data

November 12, 1999

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Angelman Syndrome
  • Binding Sites
  • Catalytic Domain
  • Conserved Sequence
  • Crystallography, X-Ray
  • Cysteine
  • Humans
  • Ligases
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Conformation
  • Protein Structure, Secondary
  • Substrate Specificity
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitins