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Article

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.

Nature - 6 Sept 2012

Plechanovová Anna, Jaffray Ellis G, Tatham Michael H, Naismith James H, Hay Ronald T

Abstract excerpt

Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked...

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Identifiers

PMID: 22842904
DOI: 10.1038/nature11376
PMCID: PMC3442243

Genes

RNF4

Provenance

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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