ArticleActa crystallographica. Section F, Structural biology communications2016
Crystal structure of a tankyrase 1-telomere repeat factor 1 complex.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Tankyrases and Their Binding Proteins: Origins of Their Roles in Diverse Cellular Pathways.Cells · 2026Review
- Tankyrase-1 regulates RBP-mediated mRNA turnover to promote muscle fiber formation.Nucleic acids research · 2024Article
- Leukocyte telomere length, allelic variations in related genes and risk of coronary heart disease in people with long-standing type 1 diabetes.Cardiovascular diabetology · 2022Article
- Review
- Tankyrases as modulators of pro-tumoral functions: molecular insights and therapeutic opportunities.Journal of experimental & clinical cancer research : CR · 2021Review
- Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity.Cellular and molecular life sciences : CMLS · 2020Review
- Structural and functional analysis of parameters governing tankyrase-1 interaction with telomeric repeat-binding factor 1 and GDP-mannose 4,6-dehydratase.The Journal of biological chemistry · 2019Article
- Poly(ADP-ribose)-dependent ubiquitination and its clinical implications.Biochemical pharmacology · 2019Review
- Telomere Length: A Potential Biomarker for the Risk and Prognosis of Stroke.Frontiers in neurology · 2019Review
- PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification.Current opinion in structural biology · 2018Review
- Structural basis for tankyrase-RNF146 interaction reveals noncanonical tankyrase-binding motifs.Protein science : a publication of the Protein Society · 2018Article
- Tankyrase1-mediated poly(ADP-ribosyl)ation of TRF1 maintains cell survival after telomeric DNA damage.Nucleic acids research · 2017Article
- Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Molecular Architecture of Full-length TRF1 Favors Its Interaction with DNA.The Journal of biological chemistry · 2016Article
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Authors and funding
7 authors.
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Abstract
Telomere repeat factor 1 (TRF1) is a subunit of shelterin (also known as the telosome) and plays a critical role in inhibiting telomere elongation by telomerase. Tankyrase 1 (TNKS1) is a poly(ADP-ribose) polymerase that regulates the activity of TRF1 through poly(ADP-ribosyl)ation (PARylation). PARylation of TRF1 by TNKS1 leads to the release of TRF1 from telomeres and allows telomerase to access telomeres. The interaction between TRF1 and TNKS1 is thus important for telomere stability and the mitotic cell cycle. Here, the crystal structure of a complex between the N-terminal acidic domain of TRF1 (residues 1-55) and a fragment of TNKS1 covering the second and third ankyrin-repeat clusters (ARC2-3) is presented at 2.2 Å resolution. The TNKS1-TRF1 complex crystals were optimized using an `oriented rescreening' strategy, in which the initial crystallization condition was used as a guide for a second round of large-scale sparse-matrix screening. This crystallographic and biochemical analysis provides a better understanding of the TRF1-TNKS1 interaction and the three-dimensional structure of the ankyrin-repeat domain of TNKS.
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