The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties.
Agel amyloidosis
Gelsolin
Misfolding
Thermal stability
X-ray crystallography
Journal
European biophysics journal : EBJ
ISSN: 1432-1017
Titre abrégé: Eur Biophys J
Pays: Germany
ID NLM: 8409413
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
received:
28
08
2019
accepted:
03
11
2019
revised:
25
10
2019
pubmed:
15
11
2019
medline:
30
9
2020
entrez:
15
11
2019
Statut:
ppublish
Résumé
Mutations in the gelsolin protein are responsible for a rare conformational disease known as AGel amyloidosis. Four of these mutations are hosted by the second domain of the protein (G2): D187N/Y, G167R and N184K. The impact of the latter has been so far evaluated only by studies on the isolated G2. Here we report the characterization of full-length gelsolin carrying the N184K mutation and compare the findings with those obtained on the wild type and the other variants. The crystallographic structure of the N184K variant in the Ca
Identifiants
pubmed: 31724080
doi: 10.1007/s00249-019-01409-9
pii: 10.1007/s00249-019-01409-9
doi:
Substances chimiques
Amyloid
0
Gelsolin
0
Calcium
SY7Q814VUP
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
11-19Références
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