ArticleNucleic acids research2016
Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Probing the dark energy in the functional protein universe.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- FKBP3 aggravates the malignant phenotype of diffuse large B-cell lymphoma by PARK7-mediated activation of Wnt/β-catenin signalling.Journal of cellular and molecular medicine · 2024Article
- Article
- Structural insights intoFrontiers in cellular and infection microbiology · 2022Review
- Tacrolimus alleviates LPS-induced AKI by inhibiting TLR4/MyD88/NF-κB signalling in mice.Journal of cellular and molecular medicine · 2022Article
- Esterase D stabilizes FKBP25 to suppress mTORC1.Cellular & molecular biology letters · 2021Article
- Mass Spectrometry-Based Redox and Protein Profiling of Failing Human Hearts.International journal of molecular sciences · 2021Article
- FKBP25 Regulates Meiotic Apparatus During Mouse Oocyte Maturation.Frontiers in cell and developmental biology · 2021Article
- FKBP9 promotes the malignant behavior of glioblastoma cells and confers resistance to endoplasmic reticulum stress inducers.Journal of experimental & clinical cancer research : CR · 2020Article
- FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020Article
- Comparative analysis of FKBP family protein: evaluation, structure, and function in mammals and Drosophila melanogaster.BMC developmental biology · 2018Review
- The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability.Nucleic acids research · 2018Article
- FKBP Ligands-Where We Are and Where to Go?Frontiers in pharmacology · 2018Review
- The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.Nucleic acids research · 2017Article
- Peptidylprolyl Isomerases as In Vivo Carriers for Drugs That Target Various Intracellular Entities.Biomolecules · 2017Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear immunophilin FKBP25 interacts with chromatin-related proteins and transcription factors and is suggested to interact with nucleic acids. Currently the structural basis of nucleic acid binding by FKBP25 is unknown. Here we determined the nuclear magnetic resonance (NMR) solution structure of full-length human FKBP25 and studied its interaction with DNA. The FKBP25 structure revealed that the N-terminal helix-loop-helix (HLH) domain and C-terminal FK506-binding domain (FKBD) interact with each other and that both of the domains are involved in DNA binding. The HLH domain forms major-groove interactions and the basic FKBD loop cooperates to form interactions with an adjacent minor-groove of DNA. The FKBP25-DNA complex model, supported by NMR and mutational studies, provides structural and mechanistic insights into the nuclear immunophilin-mediated nucleic acid recognition.
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