Glycation of glyceraldehyde-3-phosphate dehydrogenase inhibits the binding with α-synuclein and RNA.
Alpha-synuclein
Glycation
Glyceraldehyde-3-phosphate dehydrogenase
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 02 2021
15 02 2021
Historique:
received:
29
07
2020
revised:
18
12
2020
accepted:
21
12
2020
pubmed:
2
1
2021
medline:
20
2
2021
entrez:
1
1
2021
Statut:
ppublish
Résumé
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) shows great diversity of functions, interaction partners and post-translational modifications. GAPDH undergoes glycation of positively charged residues in diabetic patient's tissues and therefore may change interaction with partners. The influence of GAPDH glycation on interaction with two important partners, α-synuclein and RNA, has been investigated in silico using molecular dynamics simulations and in vitro using surface plasmon resonance measurements. Since positively charged groove including substrate- and NAD
Identifiants
pubmed: 33385367
pii: S0003-9861(20)30752-9
doi: 10.1016/j.abb.2020.108744
pii:
doi:
Substances chimiques
SNCA protein, human
0
alpha-Synuclein
0
RNA
63231-63-0
GAPDH protein, human
EC 1.2.1.12
Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)
EC 1.2.1.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108744Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.