ArticleThe Journal of biological chemistry2013
New insights into DNA recognition by zinc fingers revealed by structural analysis of the oncoprotein ZNF217.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- HBiochemistry · 2026Article
- CRISPR screening reveals ZNF217 as a vulnerability in high-risk B-cell acute lymphoblastic leukemia.Theranostics · 2025Article
- Analyzing paramagnetic NMR data on target DNA search by proteins using a discrete-state kinetic model for translocation.Biopolymers · 2024Article
- The Intricate Interplay between the ZNF217 Oncogene and Epigenetic Processes Shapes Tumor Progression.Cancers · 2022Review
- The PCOS GWAS Candidate GeneJournal of the Endocrine Society · 2022Article
- Structural basis for interaction between CLAMP and MSL2 proteins involved in the specific recruitment of the dosage compensation complex in Drosophila.Nucleic acids research · 2022Article
- ZNF213 negatively controls triple negative breast cancer progression via Hippo/YAP signaling.Cancer science · 2021Article
- Partial Deficiency of Zfp217 Resists High-Fat Diet-Induced Obesity by Increasing Energy Metabolism in Mice.International journal of molecular sciences · 2021Article
- ZNF217: the cerberus who fails to guard the gateway to lethal malignancy.American journal of cancer research · 2021Review
- Identifying regulatory pathways of spleen tyrosine kinase expression in human basophils.The Journal of allergy and clinical immunology · 2020Article
- Genomics of asthma, allergy and chronic rhinosinusitis: novel concepts and relevance in airway mucosa.Clinical and translational allergy · 2020Review
- Redox status, DNA and HSA binding study of naturally occurring naphthoquinone derivatives.EXCLI journal · 2020Article
- Improving selectivity of DNA-RNA binding zinc finger using directed evolution.BMC research notes · 2019Article
- Exploring the suitability of RanBP2-type Zinc Fingers for RNA-binding protein design.Scientific reports · 2019Article
- DNA methylation and de-methylation using hybrid site-targeting proteins.Genome biology · 2018Review
- NMR-based investigations into target DNA search processes of proteins.Methods (San Diego, Calif.) · 2018Review
- Zinc knuckle of TAF1 is a DNA binding module critical for TFIID promoter occupancy.Scientific reports · 2018Article
- Discrete-State Kinetics Model for NMR-Based Analysis of Protein Translocation on DNA at Equilibrium.The journal of physical chemistry. B · 2017Article
- Structural basis of human PR/SET domain 9 (PRDM9) allele C-specific recognition of its cognate DNA sequence.The Journal of biological chemistry · 2017Article
- Promiscuous DNA-binding of a mutant zinc finger protein corrupts the transcriptome and diminishes cell viability.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Classical zinc fingers (ZFs) are one of the most abundant and best characterized DNA-binding domains. Typically, tandem arrays of three or more ZFs bind DNA target sequences with high affinity and specificity, and the mode of DNA recognition is sufficiently well understood that tailor-made ZF-based DNA-binding proteins can be engineered. We have shown previously that a two-zinc finger unit found in the transcriptional coregulator ZNF217 recognizes DNA but with an affinity and specificity that is lower than other ZF arrays. To investigate the basis for these differences, we determined the structure of a ZNF217-DNA complex. We show that although the overall position of the ZFs on the DNA closely resembles that observed for other ZFs, the side-chain interaction pattern differs substantially from the canonical model. The structure also reveals the presence of two methyl-π interactions, each featuring a tyrosine contacting a thymine methyl group. To our knowledge, interactions of this type have not previously been described in classical ZF-DNA complexes. Finally, we investigated the sequence specificity of this two-ZF unit and discuss how ZNF217 might discriminate its target DNA sites in the cell.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.