ArticleNucleic acids research2012
The structure and selectivity of the SR protein SRSF2 RRM domain with RNA.
Article in Nucleic acids research, 2012. 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, 27 citations in OpenAlex.
- Multipurpose RNA maturation factors dysregulate multiple mRNA processing steps simultaneously and provide new therapeutic opportunities.RNA biology · 2025Review
- Biological functions of 5-methylcytosine RNA-binding proteins and their potential mechanisms in human cancers.Frontiers in oncology · 2025Review
- Integrative solution structure of PTBP1-IRES complex reveals strong compaction and ordering with residual conformational flexibility.Nature communications · 2023Article
- SRSF3/AMOTL1 splicing axis promotes the tumorigenesis of nasopharyngeal carcinoma through regulating the nucleus translocation of YAP1.Cell death & disease · 2023Article
- Article
- The rice blast fungus SR protein 1 regulates alternative splicing with unique mechanisms.PLoS pathogens · 2022Article
- Splicing factor SRSF2-centric gene regulation.International journal of biological sciences · 2021Review
- Fragment-based modelling of single stranded RNA bound to RNA recognition motif containing proteins.Nucleic acids research · 2016Article
- Antisense RNA foci in the motor neurons of C9ORF72-ALS patients are associated with TDP-43 proteinopathy.Acta neuropathologica · 2015Article
- Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function.The Biochemical journal · 2015Article
- Evolutionarily conserved exon definition interactions with U11 snRNP mediate alternative splicing regulation on U11-48K and U11/U12-65K genes.RNA biology · 2015Article
- N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation.The Biochemical journal · 2014Article
- Thermodynamic and phylogenetic insights into hnRNP A1 recognition of the HIV-1 exon splicing silencer 3 element.Biochemistry · 2014Article
- Repeat-associated RNA structure and aberrant splicing.Biochimica et biophysica acta. Gene regulatory mechanismsReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
SRSF2 is a prototypical SR protein which plays important roles in the alternative splicing of pre-mRNA. It has been shown to be involved in regulatory pathways for maintaining genomic stability and play important roles in regulating key receptors in the heart. We report here the solution structure of the RNA recognition motifs (RRM) domain of free human SRSF2 (residues 9-101). Compared with other members of the SR protein family, SRSF2 structure has a longer L3 loop region. The conserved aromatic residue in the RNP2 motif is absent in SRSF2. Calorimetric titration shows that the RNA sequence 5'AGCAGAGUA3' binds SRSF2 with a K(d) of 61 ± 1 nM and a 1:1 stoichiometry. NMR and mutagenesis experiments reveal that for SFSF2, the canonical β1 and β3 interactions are themselves not sufficient for effective RNA binding; the additional loop L3 is crucial for RNA complex formation. A comparison is made between the structures of SRSF2-RNA complex with other known RNA complexes of SR proteins. We conclude that interactions involving the L3 loop, N- and C-termini of the RRM domain are collectively important for determining selectivity between the protein and RNA.
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