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Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners

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”...

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Detalles Bibliográficos
Autores principales: Hill, Stephanie A., Kwa, Lee Gyan, Shammas, Sarah L., Lee, Jennifer C., Clarke, Jane
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9082959/
https://www.ncbi.nlm.nih.gov/pubmed/24055379
http://dx.doi.org/10.1016/j.jmb.2013.08.027
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author Hill, Stephanie A.
Kwa, Lee Gyan
Shammas, Sarah L.
Lee, Jennifer C.
Clarke, Jane
author_facet Hill, Stephanie A.
Kwa, Lee Gyan
Shammas, Sarah L.
Lee, Jennifer C.
Clarke, Jane
author_sort Hill, Stephanie A.
collection PubMed
description 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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spelling pubmed-90829592022-05-09 Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners Hill, Stephanie A. Kwa, Lee Gyan Shammas, Sarah L. Lee, Jennifer C. Clarke, Jane J Mol Biol Article 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. 2014-01-09 2013-09-17 /pmc/articles/PMC9082959/ /pubmed/24055379 http://dx.doi.org/10.1016/j.jmb.2013.08.027 Text en https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Article
Hill, Stephanie A.
Kwa, Lee Gyan
Shammas, Sarah L.
Lee, Jennifer C.
Clarke, Jane
Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title_full Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title_fullStr Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title_full_unstemmed Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title_short Mechanism of Assembly of the Non-Covalent Spectrin Tetramerization Domain from Intrinsically Disordered Partners
title_sort mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9082959/
https://www.ncbi.nlm.nih.gov/pubmed/24055379
http://dx.doi.org/10.1016/j.jmb.2013.08.027
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