The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain.
ADP-ribosyltransferase
catalytic activity
protein stability
tankyrase
zinc-binding motif
Journal
Open biology
ISSN: 2046-2441
Titre abrégé: Open Biol
Pays: England
ID NLM: 101580419
Informations de publication
Date de publication:
03 2022
03 2022
Historique:
entrez:
23
3
2022
pubmed:
24
3
2022
medline:
3
5
2022
Statut:
ppublish
Résumé
Tankyrases are ADP-ribosylating enzymes that regulate many physiological processes in the cell and are considered promising drug targets for cancer and fibrotic diseases. The catalytic ADP-ribosyltransferase domain of tankyrases contains a unique zinc-binding motif of unknown function. Recently, this motif was suggested to be involved in the catalytic activity of tankyrases. In this work, we set out to study the effect of the zinc-binding motif on the activity, stability and structure of human tankyrases. We generated mutants of human tankyrase (TNKS) 1 and TNKS2, abolishing the zinc-binding capabilities, and characterized the proteins biochemically and biophysically
Identifiants
pubmed: 35317661
doi: 10.1098/rsob.210365
pmc: PMC8941426
doi:
Substances chimiques
ADP Ribose Transferases
EC 2.4.2.-
TNKS2 protein, human
EC 2.4.2.30
Tankyrases
EC 2.4.2.30
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
210365Références
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