ArticleBiochemistry2008
Conformational changes at the tetramerization site of erythroid alpha-spectrin upon binding beta-spectrin: a spin label EPR study.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Competition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.Biochemistry · 2013Article
- 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
- Inhibition of calpain but not caspase activity by spectrin fragments.Cellular & molecular biology letters · 2010Article
- 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
- Important residue (G46) in erythroid spectrin tetramer formation.Cellular & molecular biology letters · 2010Article
- Association studies of erythroid alpha-spectrin at the tetramerization site.British journal of haematology · 2009Article
- 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.Protein science : a publication of the Protein Society · 2009Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
We used cysteine scanning, isothermal titration calorimetry (ITC) and spin label EPR methods to study the two regions that flank the partial domain Helix C' of the N-terminal end of alpha-spectrin (residues 14-20 and residues 44-54) in the absence and presence of a model protein of the beta-spectrin C-terminal end. In the absence of beta-spectrin, residues 14-20 and 46-52 were known to be unstructured. The EPR spectral values of the inverse line width (Delta H (-1)) and of the width between the low field peak and the central peak ( aZ) of residues in part of the first unstructured region (residues 17-20) and of most residues in the second unstructured junction region (residues 46-52) changed dramatically upon association with beta-spectrin, suggesting that the two regions undergo a conformational change, becoming more rigid and likely becoming helical. ITC results showed that three of the seven residues in the junction region (residues 46-52) were very important in its association with beta-spectrin, in the following order: L49 > G46 > K48. In general, our results suggest that any mutations that affect the propensity of helical formation in the region spanning residues 17-52 in alpha-spectrin, or that affect hydrophobic clustering and/or salt-bridge stabilization of the bundled helices, would affect spectrin tetramer formation, and may lead to blood disorders.
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