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

Science (New York, N.Y.) | Nov 12, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10558980

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 RIS Download

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

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