The prion protein and its ligands: Insights into structure-function relationships.
Amyloid proteins
Neurodegeneration
PrP(C)
PrP(C) ligands
PrP(C) mediated signal transduction
Prion protein
Protein aggregation
Protein misfolding
Proteolytic cleavages of cellular prion protein
shed PrP
Journal
Biochimica et biophysica acta. Molecular cell research
ISSN: 1879-2596
Titre abrégé: Biochim Biophys Acta Mol Cell Res
Pays: Netherlands
ID NLM: 101731731
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
received:
08
10
2021
revised:
23
01
2022
accepted:
28
01
2022
pubmed:
23
2
2022
medline:
19
4
2022
entrez:
22
2
2022
Statut:
ppublish
Résumé
The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that lead to prion protein fragments some of which are membrane-bound whereas others are soluble. A multitude of ligands bind to the prion protein and besides proteinaceous binding partners, interaction with metal ions and nucleic acids occurs. Although of great importance, information on structural and functional consequences of prion protein binding to its partners is limited. Here, we will reflect on the structure-function relationship of the prion protein and its binding partners considering the different folding states and prion protein fragments.
Identifiants
pubmed: 35192891
pii: S0167-4889(22)00031-3
doi: 10.1016/j.bbamcr.2022.119240
pii:
doi:
Substances chimiques
Ligands
0
Prion Proteins
0
Prions
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
119240Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.