ArticleActa crystallographica. Section F, Structural biology communications2019
A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026Article
- The gene-regulating proteins NONO and SFPQ assemble into ordered filaments.Communications biology · 2025Article
- Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation.Acta crystallographica. Section D, Structural biology · 2025Article
- Structural plasticity of the coiled-coil interactions in human SFPQ.Nucleic acids research · 2025Article
- Established and Evolving Roles of the Multifunctional Non-POU Domain-Containing Octamer-Binding Protein (NonO) and Splicing Factor Proline- and Glutamine-Rich (SFPQ).Journal of developmental biology · 2024Review
- Role of RNA binding proteins of theRNA biology · 2024Review
- Familial ALS-associatedOpen biology · 2022Article
- Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1.Nucleic acids research · 2022Article
- Binding and transport of SFPQ-RNA granules by KIF5A/KLC1 motors promotes axon survival.The Journal of cell biology · 2021Article
- The Emerging Role of the RNA-Binding Protein SFPQ in Neuronal Function and Neurodegeneration.International journal of molecular sciences · 2020Review
- Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ.Nucleic acids research · 2020Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Splicing factor proline/glutamine-rich (SFPQ) is an essential RNA-binding protein that is implicated in many aspects of nuclear function. The structures of SFPQ and two paralogs, non-POU domain-containing octamer-binding protein and paraspeckle component 1, from the Drosophila behavior human splicing protein family have previously been characterized. The unusual arrangement of the four domains, two RNA-recognition motifs (RRMs), a conserved region termed the NonA/paraspeckle (NOPS) domain and a C-terminal coiled coil, in the intertwined dimer provides a potentially unique RNA-binding surface. However, the molecular details of how the four RRMs in the dimeric SFPQ interact with RNA remain to be characterized. Here, a new crystal structure of the dimerization domain of human SFPQ in the C-centered orthorhombic space group C222
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