ArticleBiophysical journal1996
Stability of the dystrophin rod domain fold: evidence for nested repeating units.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- The atomic structure of human dystrophin spectrin-like repeat 24.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Combining Protein Expression and Molecular Data Improves Mutation Characterization of Dystrophinopathies.Frontiers in neurology · 2021Article
- Empirical and Computational Comparison of Alternative Therapeutic Exon Skip Repairs for Duchenne Muscular Dystrophy.Biochemistry · 2019Article
- 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
- The crystal structures of dystrophin and utrophin spectrin repeats: implications for domain boundaries.PloS one · 2012Article
- The polyproline site in hinge 2 influences the functional capacity of truncated dystrophins.PLoS genetics · 2010Article
- A Two-amino Acid Mutation Encountered in Duchenne Muscular Dystrophy Decreases Stability of the Rod Domain 23 (R23) Spectrin-like Repeat of Dystrophin.The Journal of biological chemistry · 2009Article
- Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy.The Journal of clinical investigation · 2009Article
- Stability of dystrophin STR fragments in relation to junction helicity.Biochimica et biophysica acta · 2008Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An examination of fragments of the human dystrophin rod domain, corresponding to a single structural repeating unit, showed that a critical chain length, defined with a precision of one residue at the C-terminal end, is required for formation of the native tertiary fold. We report here that extending the chain by six residues beyond this minimum results in a large increase in conformational stability. This is not related to a change in association state of the polypeptide. The results support the conjecture that successive repeating units in the rod domain of the spectrinlike proteins form a nested structure, in which the N-terminal part of the three-helix bundle of one repeat packs into the overlapping structure of the preceding repeat. This would be expected to affect functional characteristics related to flexibility of the dystrophin rod domain.
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Registered trials
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