Structure of an E6AP-UbcH7 Complex: Insights into Ubiquitination by the E2-E3 Enzyme Cascade
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- Lan Huang
- Cellular Biochemistry and Biophysics Program,
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- Elspeth Kinnucan
- Cellular Biochemistry and Biophysics Program,
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- Guangli Wang
- Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.
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- Sylvie Beaudenon
- Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.
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- Peter M. Howley
- Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
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- Jon M. Huibregtse
- Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.
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- Nikola P. Pavletich
- Cellular Biochemistry and Biophysics Program,
書誌事項
- 公開日
- 1999-11-12
- DOI
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- 10.1126/science.286.5443.1321
- 公開者
- American Association for the Advancement of Science (AAAS)
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説明
<jats:p>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.</jats:p>
収録刊行物
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- Science
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Science 286 (5443), 1321-1326, 1999-11-12
American Association for the Advancement of Science (AAAS)