ArticleThe Journal of biological chemistry2010
Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular consequences of SCA5 mutations in the spectrin-repeat domains of β-III-spectrin.bioRxiv : the preprint server for biology · 2024Article
- Structure and Function of RhoBTB1 Required for Substrate Specificity and Cullin-3 Ubiquitination.Function (Oxford, England) · 2023Article
- Expanding SPTAN1 monoallelic variant associated disorders: From epileptic encephalopathy to pure spastic paraplegia and ataxia.Genetics in medicine : official journal of the American College of Medical Genetics · 2023Article
- De Novo and Dominantly Inherited SPTAN1 Mutations Cause Spastic Paraplegia and Cerebellar Ataxia.Movement disorders : official journal of the Movement Disorder Society · 2022Article
- Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020Review
- The scavenger receptor SCARA1 (CD204) recognizes dead cells through spectrin.The Journal of biological chemistry · 2019Article
- Fluorescence study of the effect of cholesterol on spectrin-aminophospholipid interactions.European biophysics journal : EBJ · 2015Article
- The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap.PLoS computational biology · 2015Article
- Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.Journal of fluorescence · 2015Article
- Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.PloS one · 2015Article
- Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.Journal of molecular biology · 2014Article
- Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.Brain research · 2013Article
- Genomic approach to identify factors that drive the formation of three-dimensional structures by EA.hy926 endothelial cells.PloS one · 2013Article
- Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Biophysical journal · 2012Article
- Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization.Cellular & molecular biology letters · 2011Article
- Yeast two-hybrid and itc studies of alpha and beta spectrin interaction at the tetramerization site.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
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
We have solved the crystal structure of a segment of nonerythroid alpha-spectrin (alphaII) consisting of the first 147 residues to a resolution of 2.3 A. We find that the structure of this segment is generally similar to a corresponding segment from erythroid alpha-spectrin (alphaI) but exhibits unique differences with functional significance. Specific features include the following: (i) an irregular and frayed first helix (Helix C'); (ii) a helical conformation in the junction region connecting Helix C' with the first structural domain (D1); (iii) a long A(1)B(1) loop in D1; and (iv) specific inter-helix hydrogen bonds/salt bridges that stabilize D1. Our findings suggest that the hydrogen bond networks contribute to structural domain stability, and thus rigidity, in alphaII, and the lack of such hydrogen bond networks in alphaI leads to flexibility in alphaI. We have previously shown the junction region connecting Helix C' to D1 to be unstructured in alphaI (Park, S., Caffrey, M. S., Johnson, M. E., and Fung, L. W. (2003) J. Biol. Chem. 278, 21837-21844) and now find it to be helical in alphaII, an important difference for alpha-spectrin association with beta-spectrin in forming tetramers. Homology modeling and molecular dynamics simulation studies of the structure of the tetramerization site, a triple helical bundle of partial domain helices, show that mutations in alpha-spectrin will affect Helix C' structural flexibility and/or the junction region conformation and may alter the equilibrium between spectrin dimers and tetramers in cells. Mutations leading to reduced levels of functional tetramers in cells may potentially lead to abnormal neuronal functions.
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