ArticleProtein science : a publication of the Protein Society2009
The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: Fluorescence and molecular dynamics studies of free and bound alpha spectrin.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization.Cellular & molecular biology letters · 2011Article
- Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs.Protein science : a publication of the Protein Society · 2011Article
- Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.Blood · 2010Article
- Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation.The Journal of biological chemistry · 2010Article
- Association studies of erythroid alpha-spectrin at the tetramerization site.British journal of haematology · 2009Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The bundling of the N-terminal, partial domain helix (Helix C') of human erythroid alpha-spectrin (alphaI) with the C-terminal, partial domain helices (Helices A' and B') of erythroid beta-spectrin (betaI) to give a spectrin pseudo structural domain (triple helical bundle A'B'C') has long been recognized as a crucial step in forming functional spectrin tetramers in erythrocytes. We have used apparent polarity and Stern-Volmer quenching constants of Helix C' of alphaI bound to Helices A' and B' of betaI, along with previous NMR and EPR results, to propose a model for the triple helical bundle. This model was used as the input structure for molecular dynamics simulations for both wild type (WT) and alphaI mutant L49F. The simulation output structures show a stable helical bundle for WT, but not for L49F. In WT, four critical interactions were identified: two hydrophobic clusters and two salt bridges. However, in L49F, the region downstream of Helix C' was unable to assume a helical conformation and one critical hydrophobic cluster was disrupted. Other molecular interactions critical to the WT helical bundle were also weakened in L49F, possibly leading to the lower tetramer levels observed in patients with this mutation-induced blood disorder.
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