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Table 1 The nature and structure of polyubiquitinated and mono-ubiquitinated proteins

From: Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational modelling

Comparison list

Mono-ubiquitinated proteins

Polyubiquitinated proteins

Formation

Ubiquitin (Ub) forms a thioester to interact with E1; Ub is transferred from E1 to E2; E3 interacts with Ub-charged E2, resulting in an isopeptide bond between Ub and lysine

Ub forms a thioester to interact with E1; Ub is transferred from E1 to E2; E3 interacts with E2, which enables the conjugation between lysines and Ub chain, leading to further cycles of ubiquitination

Protein structure

Less structural disorder

More structural disorder

Ub-site structure in yeasts

More structure disorder

Less structure disorder

Ub-site structure in humans

Less structure disorder

More structure disorder

  1. E1, E2, and E3 are Ub-activating enzyme, Ub-conjugating enzyme, and ubiquitin ligase, respectively. For a comparison, see Ref [161, 162]