Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?

We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis–trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand sw...

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Detalles Bibliográficos
Autores principales: Sonnen, Andreas F.-P., Yu, Chao, Evans, Edward J., Stuart, David I., Davis, Simon J., Gilbert, Robert J.C.
Formato: Texto
Lenguaje:English
Publicado: Elsevier 2010
Materias:
Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954335/
https://www.ncbi.nlm.nih.gov/pubmed/20394753
http://dx.doi.org/10.1016/j.jmb.2010.04.011
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author Sonnen, Andreas F.-P.
Yu, Chao
Evans, Edward J.
Stuart, David I.
Davis, Simon J.
Gilbert, Robert J.C.
author_facet Sonnen, Andreas F.-P.
Yu, Chao
Evans, Edward J.
Stuart, David I.
Davis, Simon J.
Gilbert, Robert J.C.
author_sort Sonnen, Andreas F.-P.
collection PubMed
description We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis–trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits.
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spelling pubmed-29543352010-11-08 Domain Metastability: A Molecular Basis for Immunoglobulin Deposition? Sonnen, Andreas F.-P. Yu, Chao Evans, Edward J. Stuart, David I. Davis, Simon J. Gilbert, Robert J.C. J Mol Biol Communication We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis–trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits. Elsevier 2010-06-04 /pmc/articles/PMC2954335/ /pubmed/20394753 http://dx.doi.org/10.1016/j.jmb.2010.04.011 Text en © 2010 Elsevier Ltd. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Communication
Sonnen, Andreas F.-P.
Yu, Chao
Evans, Edward J.
Stuart, David I.
Davis, Simon J.
Gilbert, Robert J.C.
Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title_full Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title_fullStr Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title_full_unstemmed Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title_short Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?
title_sort domain metastability: a molecular basis for immunoglobulin deposition?
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954335/
https://www.ncbi.nlm.nih.gov/pubmed/20394753
http://dx.doi.org/10.1016/j.jmb.2010.04.011
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AT stuartdavidi domainmetastabilityamolecularbasisforimmunoglobulindeposition
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