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Article

The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.

The Journal of biological chemistry - 10 Jan 2014

Ronchi Virginia P, Klein Jennifer M, Edwards Daniel J, Haas Arthur L

Abstract excerpt

Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing forces, we propose that the fully active form of E6AP is a trimer, analysis of which reveals a buried surface of...

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Identifiers

PMID: 24273172
DOI: 10.1074/jbc.M113.517805
PMCID: PMC3887172

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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