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Article

Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.

The Journal of biological chemistry - 18 Dec 2015

Li Shengjian, Liang Yu-He, Mariano Jennifer, Metzger Meredith B, Stringer Daniel K, Hristova Ventzislava A, Li Jess, Randazzo Paul A, Tsai Yien Che, Ji Xinhua, Weissman Allan M

Abstract excerpt

RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity. We have defined, by co-crystallization, the distinctive means by which AO7 binds UbcH5B. AO7 contains a structurally unique UbcH5B binding region (U5BR) that is connected by an 11-amino acid linker to its RING domain, forming...

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Identifiers

PMID: 26475854
DOI: 10.1074/jbc.M115.685867
PMCID: PMC4683248

Genes

RNF25

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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