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Article

Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity.

The Journal of biological chemistry - 12 Nov 2010

Ko Sunggeon, Kang Gil Bu, Song Sung Min, Lee Jung-Gyu, Shin Dong Yeon, Yun Ji-Hye, Sheng Yi, Cheong Chaejoon, Jeon Young Ho, Jung Yong-Keun, Arrowsmith Cheryl H, Avvakumov George V, Dhe-Paganon Sirano, Yoo Yung Joon, Eom Soo Hyun, Lee Weontae

Abstract excerpt

E2-25K/Hip2 is an unusual ubiquitin-conjugating enzyme that interacts with the frameshift mutant of ubiquitin B (UBB(+1)) and has been identified as a crucial factor regulating amyloid-β neurotoxicity. To study the structural basis of the neurotoxicity mediated by the E2-25K-UBB(+1) interaction, we determined the three-dimensional structures of UBB(+1), E2-25K and the E2-25K/ubiquitin, and E2-25K/UBB(+1) complex....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20826778
DOI: 10.1074/jbc.M110.145219
PMCID: PMC2975229

Genes

UBB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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