The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain

S A Kozin; A A Kulikova; A N Istrate; P O Tsvetkov; S S Zhokhov; Y V Mezentsev; O I Kechko; A S Ivanov; V I Polshakov; A A Makarov

doi:10.1039/c4mt00259h

The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain

Metallomics. 2015 Mar;7(3):422-5. doi: 10.1039/c4mt00259h.

Authors

S A Kozin¹, A A Kulikova, A N Istrate, P O Tsvetkov, S S Zhokhov, Y V Mezentsev, O I Kechko, A S Ivanov, V I Polshakov, A A Makarov

Affiliation

¹ Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov street 32, 119991 Moscow, Russia. aamakarov@eimb.ru.

PMID: 25703165
DOI: 10.1039/c4mt00259h

Abstract

Interaction of Zn(2+) with the metal-binding domain of the English (H6R) amyloid-β mutant results in the formation of peptide dimers. The mutation causes the exclusion of His6 from the zinc chelation pattern observed in the intact domain and triggers the assembly of the dimers via zinc ions coordinated by (11)EVHH(14) fragments.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alzheimer Disease / genetics*
Amyloid beta-Peptides / chemistry*
Amyloid beta-Peptides / genetics*
Amyloid beta-Peptides / metabolism
Calorimetry
England
Humans
Mutation / genetics*
Protein Binding / drug effects
Protein Multimerization / drug effects*
Protein Structure, Tertiary
Proton Magnetic Resonance Spectroscopy
Surface Plasmon Resonance
Zinc / pharmacology*

Substances

Amyloid beta-Peptides
Zinc