---

Huang L, et al.  (1999) Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286(5443):1321-6

Abstract: 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.

Status: Published

Type: Journal Article

PubMed ID: 10558980

---

Author Searches

To find contact information or other publications by the authors of this paper, follow these three steps:

1. (1) Choose an author,
2. (2) Choose a search parameter,
3. (3) Click to implement

Huang L Kinnucan E Wang G Beaudenon S Howley PM Huibregtse JM Pavletich NP Papers in SGD Colleagues in SGD PubMed Google Scholar

---