The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain
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, thi...
Main Authors: | Sven T. Sowa, Lari Lehtiö |
---|---|
Format: | Article |
Language: | English |
Published: |
The Royal Society
2022-03-01
|
Series: | Open Biology |
Subjects: | |
Online Access: | https://royalsocietypublishing.org/doi/10.1098/rsob.210365 |
Similar Items
-
TBM Hunter: Identify and Score Canonical, Extended, and Unconventional Tankyrase-Binding Motifs in Any Protein
by: Christopher M. Clements, et al.
Published: (2023-11-01) -
Research Progress on Mono-ADP-Ribosyltransferases in Human Cell Biology
by: Yujie Gan, et al.
Published: (2022-05-01) -
An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases
by: Sven T. Sowa, et al.
Published: (2022-11-01) -
Broad-Spectrum Regulation of Nonreceptor Tyrosine Kinases by the Bacterial ADP-Ribosyltransferase EspJ
by: Dominic J. Pollard, et al.
Published: (2018-05-01) -
A novel predicted ADP-ribosyltransferase-like family conserved in eukaryotic evolution
by: Zbigniew Wyżewski, et al.
Published: (2021-03-01)