ArticleProtein science : a publication of the Protein Society2011
Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 57 citations in OpenAlex.
- Multidomain Coupling Governs FoxP1 Assembly and Nuclear Compartmentalization.bioRxiv : the preprint server for biology · 2026Article
- FOXP Transcription Factors in Thyroid Cancer: From Molecular Expression to Clinical Significance.Biomedicines · 2026Review
- Examining Genetic Variants Associated with FOXP1 Syndrome through Molecular Dynamics of Its DNA-Binding Domain and Self-Organizing Maps.Journal of chemical information and modeling · 2026Article
- Multimerizing transcription factors FOXP3 and AIRE as chromatin architectural regulators.Nature immunology · 2026Review
- DNA controls the dimerization of the human FoxP1 forkhead domain.Cell reports. Physical science · 2024Article
- Deacetylation of FOXP1 by HDAC7 potentiates self-renewal of mesenchymal stem cells.Stem cell research & therapy · 2023Article
- DNA facilitates heterodimerization between human transcription factors FoxP1 and FoxP2 by increasing their conformational flexibility.iScience · 2023Article
- Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1.The Journal of chemical physics · 2023Article
- Article
- Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein.Biophysical journal · 2021Article
- Toward a mechanistic understanding of DNA binding by forkhead transcription factors and its perturbation by pathogenic mutations.Nucleic acids research · 2021Review
- Individuals with FOXP1 syndrome present with a complex neurobehavioral profile with high rates of ADHD, anxiety, repetitive behaviors, and sensory symptoms.Molecular autism · 2021Article
- Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping.International journal of molecular sciences · 2021Review
- Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.PloS one · 2021Article
- Intrinsically Disordered Regions of the DNA-Binding Domain of Human FoxP1 Facilitate Domain Swapping.Journal of molecular biology · 2020Article
- Molecular networks of FOXP family: dual biologic functions, interplay with other molecules and clinical implications in cancer progression.Molecular cancer · 2019Review
- Crystal Structure of FOXC2 in Complex with DNA Target.ACS omega · 2019Article
- Dissecting FOXP2 Oligomerization and DNA Binding.Angewandte Chemie (International ed. in English) · 2019Article
- The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1.Scientific reports · 2019Article
- Methylation Marks of Blood Leukocytes of Native Hucul Mares Differentiated in Age.International journal of genomics · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FOXP1 belongs to the P-subfamily of forkhead transcription factors and contains a conserved forkhead DNA-binding domain. According to size exclusion chromatography analysis, the forkhead domain of FOXP1 existed as a mixture of monomer and dimer. The dissociation constants of the forkhead domain of wild-type, C61S, and C61Y mutants of FOXP1 were 27.3, 28.8, and 332.0 μM, respectively. In contrast, FOXP1 A39P mutant formed only a monomer. NMR analysis also showed that FOXP1 C61S and C61Y mutants existed as a mixture. The solution structure of FOXP1 A39P/C61Y mutant was similar to the X-ray structure of the FOXP2 monomer. Comparison of backbone dynamics of FOXP1 A39P/C61Y and C61Y mutants showed that the residues preceding helix 3, the hinge region, exhibited the largest conformational exchange in FOXP1 monomer. The A39 residue of FOXP1 dimer has a lower order parameter with internal motion on the ps-ns timescale, suggesting that the dynamics of the hinge region of FOXP1 are important in the formation of the swapped dimer. The analysis also showed that the residues exhibiting the motions on the ps-ns and μs-ms timescales were located at the DNA-binding surface of FOXP1, suggesting the interactions between FOXP1 and DNA may be highly dynamic.
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