ArticleProceedings of the National Academy of Sciences of the United States of America1991
Phasing the conformational unit of spectrin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Journal of molecular biology · 2014Article
- Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.Journal of molecular biology · 2012Article
- Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanisms.Journal of molecular biology · 2009Article
- 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
- Molecular epitopes of the ankyrin-spectrin interaction.Biochemistry · 2008Article
- Spectrin domains lose cooperativity in forced unfolding.Biophysical journal · 2007Article
- Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.Biophysical journal · 2006Article
- Complex folding kinetics of a multidomain protein.Biophysical journal · 2006Article
- Extending a spectrin repeat unit. II: rupture behavior.Biophysical journal · 2006Article
- Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Caenorhabditis elegans beta-G spectrin is dispensable for establishment of epithelial polarity, but essential for muscular and neuronal function.The Journal of cell biology · 2000Article
- Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis.The Biochemical journal · 1998Article
- Drosophila development requires spectrin network formation.The Journal of cell biology · 1995Article
- Interchain binding at the tail end of the Drosophila spectrin molecule.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Identification of the vinculin-binding site in the cytoskeletal protein alpha-actinin.The Biochemical journal · 1994Article
- Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster.The Journal of cell biology · 1993Article
- Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46.The Journal of clinical investigation · 1993Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Many proteins contain a repetitive sequence motif, which implies that they contain a repetitive structural motif. Spectrin and the related proteins dystrophin and alpha-actinin consist largely of repeated motifs of 100-120 residues. But the repeating motif is degenerate and it has been difficult to define the boundaries of the repeating sequence unit or its corresponding structural unit. We have determined at which residues the structural units that correspond to spectrin's repeating 106-amino acid motifs begin and end. Drosophila alpha-spectrin cDNAs were expressed in bacteria to show that single segments (106 amino acids) and pairs of segments encoded by selected regions of spectrin cDNA can fold into stable conformations whose biophysical and biochemical properties are similar to those of native spectrin. Because such folding was critically dependent on the phasing of the expressed sequence with respect to the apparent boundaries of the repeating motifs, our data provide experimental evidence that relates the boundaries of the folded, conformational unit to the chemical sequence of repeating motifs.
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