ArticleThe Journal of biological chemistry2015
Structural Basis of Neuronal Nitric-oxide Synthase Interaction with Dystrophin Repeats 16 and 17.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- N-terminal titin fragment: a non-invasive, pharmacodynamic biomarker for microdystrophin efficacy.Skeletal muscle · 2024Article
- Dystrophin- and Utrophin-Based Therapeutic Approaches for Treatment of Duchenne Muscular Dystrophy: A Comparative Review.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2024Review
- When SizeBiomedicines · 2023Article
- The X-linked Becker muscular dystrophy (bmx) mouse models Becker muscular dystrophy via deletion of murine dystrophin exons 45-47.Journal of cachexia, sarcopenia and muscle · 2023Article
- Review
- Effects of Mini-Dystrophin on Dystrophin-Deficient, Human Skeletal Muscle-Derived Cells.International journal of molecular sciences · 2020Article
- Longitudinal metabolomic analysis of plasma enables modeling disease progression in Duchenne muscular dystrophy mouse models.Human molecular genetics · 2020Article
- Restoration of Functional Full-Length Dystrophin After Intramuscular Transplantation of Foamy Virus-Transduced Myoblasts.Human gene therapy · 2020Article
- Exons 45-55 Skipping Using Mutation-Tailored Cocktails of Antisense Morpholinos in the DMD Gene.Molecular therapy : the journal of the American Society of Gene Therapy · 2019Article
- Dystrophin deficiency leads to dysfunctional glutamate clearance in iPSC derived astrocytes.Translational psychiatry · 2019Article
- Dystrophin R16/17-syntrophin PDZ fusion protein restores sarcolemmal nNOSμ.Skeletal muscle · 2018Article
- CRISPR-Induced Deletion with SaCas9 Restores Dystrophin Expression in Dystrophic Models In Vitro and In Vivo.Molecular therapy : the journal of the American Society of Gene Therapy · 2018Article
- Relation of nNOS isoforms to mitochondrial density and PGC-1alpha expression in striated muscles of mice.Nitric oxide : biology and chemistry · 2018Article
- Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.The Journal of biological chemistry · 2018Article
- miR-708-5p and miR-34c-5p are involved in nNOS regulation in dystrophic context.Skeletal muscle · 2018Article
- Muscle Weakness in Rheumatoid Arthritis: The Role of CaEBioMedicine · 2017Review
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Duchenne muscular dystrophy is a lethal genetic defect that is associated with the absence of dystrophin protein. Lack of dystrophin protein completely abolishes muscular nitric-oxide synthase (NOS) function as a regulator of blood flow during muscle contraction. In normal muscles, nNOS function is ensured by its localization at the sarcolemma through an interaction of its PDZ domain with dystrophin spectrin-like repeats R16 and R17. Early studies suggested that repeat R17 is the primary site of interaction but ignored the involved nNOS residues, and the R17 binding site has not been described at an atomic level. In this study, we characterized the specific amino acids involved in the binding site of nNOS-PDZ with dystrophin R16-17 using combined experimental biochemical and structural in silico approaches. First, 32 alanine-scanning mutagenesis variants of dystrophin R16-17 indicated the regions where mutagenesis modified the affinity of the dystrophin interaction with the nNOS-PDZ. Second, using small angle x-ray scattering-based models of dystrophin R16-17 and molecular docking methods, we generated atomic models of the dystrophin R16-17·nNOS-PDZ complex that correlated well with the alanine scanning identified regions of dystrophin. The structural regions constituting the dystrophin interaction surface involve the A/B loop and the N-terminal end of helix B of repeat R16 and the N-terminal end of helix A' and a small fraction of helix B' and a large part of the helix C' of repeat R17. The interaction surface of nNOS-PDZ involves its main β-sheet and its specific C-terminal β-finger.
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