ArticleThe Biochemical journal2012
Solution structure of the core SMN-Gemin2 complex.
Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Rare SMA Patients: A Comprehensive Look at Clinical Features, Genetic Profiles and Therapeutic Approaches.International journal of molecular sciences · 2026Article
- Spinal muscular atrophy: Biology, pathogenesis, and therapeutic advances.Therapeutic advances in neurological disorders · 2026Review
- The survival motor neuron protein: structure, functions, stability, and therapeutic targeting.Frontiers in cellular neuroscience · 2026Review
- Structural Impact of Ex Vivo Resistance Mutations on HIV-1 Integrase Polymers Induced by Allosteric Inhibitors.Journal of molecular biology · 2025Article
- Ubiquitination Insight from Spinal Muscular Atrophy-From Pathogenesis to Therapy: A Muscle Perspective.International journal of molecular sciences · 2024Review
- Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast.iScience · 2023Article
- Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization.PLoS pathogens · 2023Article
- SMA-linked SMN mutants prevent phase separation properties and SMN interactions with FMRP family members.Life science alliance · 2023Article
- RNA binding proteins (RBPs) and their role in DNA damage and radiation response in cancer.Advanced drug delivery reviews · 2022Review
- New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response.Frontiers in molecular biosciences · 2021Review
- SMN - A chaperone for nuclear RNP social occasions?RNA biology · 2017Review
- Diverse role of survival motor neuron protein.Biochimica et biophysica acta. Gene regulatory mechanisms · 2017Review
- How do SMA-linked mutations of SMN1 lead to structural/functional deficiency of the SMA protein?PloS one · 2017Article
- A new communication hub in the RNA world.Nature structural & molecular biology · 2016Article
- Oligomeric Properties of Survival Motor Neuron·Gemin2 Complexes.The Journal of biological chemistry · 2015Article
- Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.The EMBO journal · 2015Article
- Intrinsically disordered proteins in the nucleus of human cells.Biochemistry and biophysics reports · 2015Article
- Assays for the identification and prioritization of drug candidates for spinal muscular atrophy.Assay and drug development technologies · 2014Review
- Identification of truncated forms of U1 snRNA reveals a novel RNA degradation pathway during snRNP biogenesis.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
In humans, assembly of spliceosomal snRNPs (small nuclear ribonucleoproteins) begins in the cytoplasm where the multi-protein SMN (survival of motor neuron) complex mediates the formation of a seven-membered ring of Sm proteins on to a conserved site of the snRNA (small nuclear RNA). The SMN complex contains the SMN protein Gemin2 and several additional Gemins that participate in snRNP biosynthesis. SMN was first identified as the product of a gene found to be deleted or mutated in patients with the neurodegenerative disease SMA (spinal muscular atrophy), the leading genetic cause of infant mortality. In the present study, we report the solution structure of Gemin2 bound to the Gemin2-binding domain of SMN determined by NMR spectroscopy. This complex reveals the structure of Gemin2, how Gemin2 binds to SMN and the roles of conserved SMN residues near the binding interface. Surprisingly, several conserved SMN residues, including the sites of two SMA patient mutations, are not required for binding to Gemin2. Instead, they form a conserved SMN/Gemin2 surface that may be functionally important for snRNP assembly. The SMN-Gemin2 structure explains how Gemin2 is stabilized by SMN and establishes a framework for structure-function studies to investigate snRNP biogenesis as well as biological processes involving Gemin2 that do not involve snRNP assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.