ArticleJournal of molecular biology2014
Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed.
- Severe SPTBN4-Related Neurodevelopmental Disorder: Case Report of Two Siblings with Lethal Outcomes.Journal of molecular neuroscience : MN · 2026Article
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- De Novo and Dominantly Inherited SPTAN1 Mutations Cause Spastic Paraplegia and Cerebellar Ataxia.Movement disorders : official journal of the Movement Disorder Society · 2022Article
- αI-spectrin represents evolutionary optimization of spectrin for red blood cell deformability.Biophysical journal · 2021Article
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Binding-induced folding under unfolding conditions: Switching between induced fit and conformational selection mechanisms.The Journal of biological chemistry · 2019Article
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Residual Structure Accelerates Binding of Intrinsically Disordered ACTR by Promoting Efficient Folding upon Encounter.Journal of molecular biology · 2019Article
- A Supramolecular Polymerization Approach to the Growth of the Myofibril.Frontiers in chemistry · 2019Article
- Folding and binding pathways of BH3-only proteins are encoded within their intrinsically disordered sequence, not templated by partner proteins.The Journal of biological chemistry · 2018Article
- How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?Biophysical journal · 2018Article
- pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Biophysical journal · 2017Article
- Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.The Journal of biological chemistry · 2016Review
- Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein.Scientific reports · 2016Article
- Quarterly intrinsic disorder digest (January-February-March, 2014).Intrinsically disordered proteins · 2016Article
- Protein folding in the cell, from atom to organism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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5 authors.
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Abstract
Interdomain interactions of spectrin are critical for maintenance of the erythrocyte cytoskeleton. In particular, "head-to-head" dimerization occurs when the intrinsically disordered C-terminal tail of β-spectrin binds the N-terminal tail of α-spectrin, folding to form the "spectrin tetramer domain". This non-covalent three-helix bundle domain is homologous in structure and sequence to previously studied spectrin domains. We find that this tetramer domain is surprisingly kinetically stable. Using a protein engineering Φ-value analysis to probe the mechanism of formation of this tetramer domain, we infer that the domain folds by the docking of the intrinsically disordered β-spectrin tail onto the more structured α-spectrin tail.
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