7YSF

Crystal structure of ZNF524 ZF1-4 in complex with telomeric DNA

Summary for 7YSF

• Entry DOI: 10.2210/pdb7ysf/pdb
• Descriptor: Zinc finger protein 524, DNA (5'-D(*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*TP*TP*AP*GP*G)-3'), DNA (5'-D(*TP*CP*CP*TP*AP*AP*CP*CP*CP*TP*AP*AP*CP*CP*C)-3'), ... (6 entities in total)
• Functional Keywords: c2h2 zinc finger, dna binding protein, transferase-dna complex, transferase/dna
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 25163.91

Authors

Li, F.D.,Xu, Z.Y. (deposition date: 2022-08-12, release date: 2023-08-16, Last modification date: 2024-04-24)

Primary citation

Braun, H.,Xu, Z.,Chang, F.,Viceconte, N.,Rane, G.,Levin, M.,Lototska, L.,Roth, F.,Hillairet, A.,Fradera-Sola, A.,Khanchandani, V.,Sin, Z.W.,Yong, W.K.,Dreesen, O.,Yang, Y.,Shi, Y.,Li, F.,Butter, F.,Kappei, D.
ZNF524 directly interacts with telomeric DNA and supports telomere integrity.
Nat Commun, 14:8252-8252, 2023

PubMed Abstract: Telomeres are nucleoprotein structures at the ends of linear chromosomes. In humans, they consist of TTAGGG repeats, which are bound by dedicated proteins such as the shelterin complex. This complex blocks unwanted DNA damage repair at telomeres, e.g. by suppressing nonhomologous end joining (NHEJ) through its subunit TRF2. Here, we describe ZNF524, a zinc finger protein that directly binds telomeric repeats with nanomolar affinity, and reveal base-specific sequence recognition by cocrystallization with telomeric DNA. ZNF524 localizes to telomeres and specifically maintains the presence of the TRF2/RAP1 subcomplex at telomeres without affecting other shelterin members. Loss of ZNF524 concomitantly results in an increase in DNA damage signaling and recombination events. Overall, ZNF524 is a direct telomere-binding protein involved in the maintenance of telomere integrity.

PubMed: 38086788
DOI: 10.1038/s41467-023-43397-7

Experimental method

X-RAY DIFFRACTION (2.4 Å)