How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?


Journal

Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788

Informations de publication

Date de publication:
02 2019
Historique:
received: 18 08 2018
revised: 19 11 2018
accepted: 21 11 2018
pubmed: 12 12 2018
medline: 18 12 2019
entrez: 12 12 2018
Statut: ppublish

Résumé

Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the -PHGGGWGQ- octapeptide sequence. This octarepeat domain can bind up to four Cu

Identifiants

pubmed: 30529722
pii: S0162-0134(18)30493-8
doi: 10.1016/j.jinorgbio.2018.11.012
pii:
doi:

Substances chimiques

Membrane Lipids 0
Micelles 0
Sodium Dodecyl Sulfate 368GB5141J
Copper 789U1901C5

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

143-153

Informations de copyright

Copyright © 2018 Elsevier Inc. All rights reserved.

Auteurs

Aleksandra Hecel (A)

Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50383 Wroclaw, Poland. Electronic address: aleksandra.hecel@chem.uni.wroc.pl.

Daniela Valensin (D)

Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A. Moro 2, 53100 Siena, Italy.

Henryk Kozłowski (H)

Opole Medical School in Opole, Katowicka 68, 45060 Opole, Poland.

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Classifications MeSH