ArticleProtein science : a publication of the Protein Society2008
The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein.
Article in Protein science : a publication of the Protein Society, 2008. 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, 22 citations in OpenAlex.
- BAGEL: Protein engineering via exploration of an energy landscape.PLoS computational biology · 2025Article
- ZNF593 regulates the cGAS-mediated innate immune response by attenuating cGAS-DNA binding.Cell death and differentiation · 2025Article
- Half a Century of Progress: The Evolution of Wheat Germ-Based In Vitro Translation into a Versatile Protein Production Method.International journal of molecular sciences · 2025Review
- Zinc finger protein 593 promotes breast cancer development by ensuring DNA damage repair and cell-cycle progression.iScience · 2024Article
- Reduction of ZFX levels decreases histone H4 acetylation and increases Pol2 pausing at target promoters.Nucleic acids research · 2024Article
- Copy number variants suggest different molecular pathways for the pathogenesis of bladder exstrophy.American journal of medical genetics. Part A · 2023Article
- Binding cavities and druggability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2015Article
- Papillomavirus binding factor (PBF) is an intrinsically disordered protein with potential participation in osteosarcoma genesis, in silico evidence.Theoretical biology & medical modelling · 2014Article
- The conserved Bud20 zinc finger protein is a new component of the ribosomal 60S subunit export machinery.Molecular and cellular biology · 2012Article
- A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins.Journal of biomolecular NMR · 2012Article
- Targeted proteomics reveals compositional dynamics of 60S pre-ribosomes after nuclear export.Molecular systems biology · 2012Article
- A fortuitous insight into a common mode of RNA recognition by the dsRNA-specific zinc fingers.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- High-yield expression in E. coli and refolding of the bZIP domain of activating transcription factor 5.Protein expression and purification · 2008Article
- Zinc finger structure determination by NMR: Why zinc fingers can be a handful.Progress in nuclear magnetic resonance spectroscopyReview
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Here, we report the solution structure of ZNF593, a protein identified in a functional study as a negative modulator of the DNA-binding activity of the Oct-2 transcription factor. ZNF593 contains a classic C(2)H(2) zinc finger domain flanked by about 40 disordered residues on each terminus. Although the protein contains a high degree of intrinsic disorder, the structure of the zinc finger domain was resolved by NMR spectroscopy without a need for N- or C-terminal truncations. The tertiary structure of the zinc finger domain is composed of a beta-hairpin that positions the cysteine side chains for zinc coordination, followed by an atypical kinked alpha-helix containing the two histidine side chain ligands. The structural topology of ZNF593 is similar to a fragment of the double-stranded RNA-binding protein Zfa and the C-terminal zinc finger of MBP-1, a human enhancer binding protein. The structure presented here will provide a guide for future functional studies of how ZNF593 negatively modulates the DNA-binding activity of Oct-2, a POU domain-containing transcription factor. Our work illustrates the unique capacity of NMR spectroscopy for structural analysis of folded domains in a predominantly disordered protein.
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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.