Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR
The p53-binding protein 1 (53BP1) regulates the choice of the DNA double-strand break repair pathway. Here the authors present the crystal structure of Tudor-interacting repair regulator (TIRR) bound to the 53BP1 tandem Tudor domain, which reveals how TIRR blocks H4K20me2 binding to 53BP1 Tudor and...
Saved in:
Main Authors: | Yaxin Dai, Aili Zhang, Shan Shan, Zihua Gong, Zheng Zhou |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2018
|
Subjects: | |
Online Access: | https://doaj.org/article/10e5474c6f744b3e827891e12f49cc88 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR
by: Jiaxu Wang, et al.
Published: (2018) -
Author Correction: Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR
by: Jiaxu Wang, et al.
Published: (2019) -
Discovery of small molecules targeting the tandem tudor domain of the epigenetic factor UHRF1 using fragment-based ligand discovery
by: Lyra Chang, et al.
Published: (2021) -
Molecular recognition of H3/H4 histone tails by the tudor domains of JMJD2A: a comparative molecular dynamics simulations study.
by: Musa Ozboyaci, et al.
Published: (2011) -
Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors
by: Pau Martin-Malpartida, et al.
Published: (2017)