ArticlePloS one2012
The crystal structures of dystrophin and utrophin spectrin repeats: implications for domain boundaries.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- The atomic structure of human dystrophin spectrin-like repeat 24.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Article
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
- Combining Protein Expression and Molecular Data Improves Mutation Characterization of Dystrophinopathies.Frontiers in neurology · 2021Article
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- Development of Novel Micro-dystrophins with Enhanced Functionality.Molecular therapy : the journal of the American Society of Gene Therapy · 2019Article
- Syntrophins entangled in cytoskeletal meshwork: Helping to hold it all together.Cell proliferation · 2019Review
- Fine mapping of hydrophobic contacts reassesses the organization of the first three dystrophin coiled-coil repeats.Protein science : a publication of the Protein Society · 2019Article
- Syntrophin binds directly to multiple spectrin-like repeats in dystrophin and mediates binding of nNOS to repeats 16-17.Human molecular genetics · 2018Article
- Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.The Journal of biological chemistry · 2018Article
- Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin.PLoS computational biology · 2018Article
- Investigating Synthetic Oligonucleotide Targeting of Mir31 in Duchenne Muscular Dystrophy.PLoS currents · 2016Article
- Reinforcing the LINC complex connection to actin filaments: the role of FHOD1 in TAN line formation and nuclear movement.Cell cycle (Georgetown, Tex.) · 2015Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dystrophin and utrophin link the F-actin cytoskeleton to the cell membrane via an associated glycoprotein complex. This functionality results from their domain organization having an N-terminal actin-binding domain followed by multiple spectrin-repeat domains and then C-terminal protein-binding motifs. Therapeutic strategies to replace defective dystrophin with utrophin in patients with Duchenne muscular dystrophy require full-characterization of both these proteins to assess their degree of structural and functional equivalence. Here the high resolution structures of the first spectrin repeats (N-terminal repeat 1) from both dystrophin and utrophin have been determined by x-ray crystallography. The repeat structures both display a three-helix bundle fold very similar to one another and to homologous domains from spectrin, α-actinin and plectin. The utrophin and dystrophin repeat structures reveal the relationship between the structural domain and the canonical spectrin repeat domain sequence motif, showing the compact structural domain of spectrin repeat one to be extended at the C-terminus relative to its previously defined sequence repeat. These structures explain previous in vitro biochemical studies in which extending dystrophin spectrin repeat domain length leads to increased protein stability. Furthermore we show that the first dystrophin and utrophin spectrin repeats have no affinity for F-actin in the absence of other domains.
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