ArticleProtein science : a publication of the Protein Society2007
Solution structure of the zinc finger HIT domain in protein FON.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- Activity of the mammalian DNA transposon piggyBat from Myotis lucifugus is restricted by its own transposon ends.Nature communications · 2025Article
- CryoEM of RUVBL1-RUVBL2-ZNHIT2, a complex that interacts with pre-mRNA-processing-splicing factor 8.Nucleic acids research · 2022Article
- A long non-coding RNA (Lrap) modulates brain gene expression and levels of alcohol consumption in rats.Genes, brain, and behavior · 2021Review
- Crystal structures of REF6 and its complex with DNA reveal diverse recognition mechanisms.Cell discovery · 2020Article
- R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein.Nature communications · 2017Article
- Expression proteomics study to determine metallodrug targets and optimal drug combinations.Scientific reports · 2017Article
- A novel zinc-finger HIT protein with an additional PAPA-1-like region from Suaeda liaotungensis K. enhanced transgenic Arabidopsis drought and salt stresses tolerance.Molecular biotechnology · 2014Article
- New insights into the biogenesis of nuclear RNA polymerases?Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Nuclear receptor-coregulator interaction profiling identifies TRIP3 as a novel peroxisome proliferator-activated receptor gamma cofactor.Molecular & cellular proteomics : MCP · 2009Article
- 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
15 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The zinc finger HIT domain is a sequence motif found in many proteins, including thyroid hormone receptor interacting protein 3 (TRIP-3), which is possibly involved in maturity-onset diabetes of the young (MODY). Novel zinc finger motifs are suggested to play important roles in gene regulation and chromatin remodeling. Here, we determined the high-resolution solution structure of the zinc finger HIT domain in ZNHIT2 (protein FON) from Homo sapiens, by an NMR method based on 567 upper distance limits derived from NOE intensities measured in three-dimensional NOESY spectra. The structure yielded a backbone RMSD to the mean coordinates of 0.19 A for the structured residues 12-48. The fold consists of two consecutive antiparallel beta-sheets and two short C-terminal helices packed against the second beta-sheet, and binds two zinc ions. Both zinc ions are coordinated tetrahedrally via a CCCC-CCHC motif to the ligand residues of the zf-HIT domain in an interleaved manner. The tertiary structure of the zinc finger HIT domain closely resembles the folds of the B-box, RING finger, and PHD domains with a cross-brace zinc coordination mode, but is distinct from them. The unique three-dimensional structure of the zinc finger HIT domain revealed a novel zinc-binding fold, as a new member of the treble clef domain family. On the basis of the structural data, we discuss the possible functional roles of the zinc finger HIT domain.
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