1c4z

From Proteopedia

---

Revision as of 14:10, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1c4z, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Angelman syndrome OMIM:[601623]

About this Structure

1C4Z is a Protein complex structure of sequences from Homo sapiens. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

Reference

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade., Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP, Science. 1999 Nov 12;286(5443):1321-6. PMID:10558980

Page seeded by OCA on Mon Nov 12 16:17:23 2007