XRD1 Highlights

Single-point mutation, metal ion concentration and low dielectric constant of the medium induce human ubiquitin aggregation

Ribbon representation of the asymmetric unit content (chains A,B and C) plus one symmetriy-related molecule of chain B (B*), of E16V crystal grown at 35 mM Zn2+. The metal sites (ZN1, Zn5, Zn6 and Zn7) are represented as yellow spheres. The side chain of the mutated residue (Val16) is shown as red sticks

Fermani S et al, Chem. Eur. J., 2017, 24, pp 4140

Human ubiquitin (hUb) is a small and stable globular protein involved in several aspects of cell physiology. Interest in aggregation pathways of human ubiquitin (hUb) stems from hUb-positive aggregates being biomarkers of neurodegenerative diseases. Two hUb dimers have been recognized as possible precursors of amyloid-like aggregates, but their formation is disfavored by electrostatic repulsions involving mainly Glu16. Substitution of Glu16 negative charge by a metal ion and a decrease of the dielectric constant of the medium can also induce hUb aggregation
Retrieve Article

Aggregation Pathways of Native‐Like Ubiquitin Promoted by Single‐Point Mutation, Metal Ion Concentration, and Dielectric Constant of the Medium;
Fermani S, Calvaresi M, Mangini V, Falini G, Bottoni A, Natile G, Arnesano F, Chem. Eur. J., 2018, 24, pp 4140
DOI: 10.1002/chem.201705543

Last Updated on Monday, 22 May 2023 15:31