3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins

Among thousands of homo-oligomeric protein structures, there is a small but growing subset of ‘domain-swapped’ proteins. The term ‘domain swapping,’ originally coined by D. Eisenberg, describes a scenario in which two or more polypeptide chains exchange identical units for oligomerization. This type...

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Detalles Bibliográficos
Autores principales: Liu, L., Gronenborn, A.M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7152442/
http://dx.doi.org/10.1016/B978-0-12-374920-8.00309-X
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author Liu, L.
Gronenborn, A.M.
author_facet Liu, L.
Gronenborn, A.M.
author_sort Liu, L.
collection PubMed
description Among thousands of homo-oligomeric protein structures, there is a small but growing subset of ‘domain-swapped’ proteins. The term ‘domain swapping,’ originally coined by D. Eisenberg, describes a scenario in which two or more polypeptide chains exchange identical units for oligomerization. This type of assembly could play a role in disease-related aggregation and amyloid formation or as a specific mechanism for regulating function. This chapter introduces terms and features concerning domain swapping, summarizes ideas about its putative mechanisms, reports on domain-swapped structures collected from the literature, and describes a few notable examples in detail.
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spelling pubmed-71524422020-04-13 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins Liu, L. Gronenborn, A.M. Comprehensive Biophysics Article Among thousands of homo-oligomeric protein structures, there is a small but growing subset of ‘domain-swapped’ proteins. The term ‘domain swapping,’ originally coined by D. Eisenberg, describes a scenario in which two or more polypeptide chains exchange identical units for oligomerization. This type of assembly could play a role in disease-related aggregation and amyloid formation or as a specific mechanism for regulating function. This chapter introduces terms and features concerning domain swapping, summarizes ideas about its putative mechanisms, reports on domain-swapped structures collected from the literature, and describes a few notable examples in detail. 2012 2012-05-03 /pmc/articles/PMC7152442/ http://dx.doi.org/10.1016/B978-0-12-374920-8.00309-X Text en Copyright © 2012 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Liu, L.
Gronenborn, A.M.
3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title_full 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title_fullStr 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title_full_unstemmed 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title_short 3.8 Protein and Nucleic Acid Folding: Domain Swapping in Proteins
title_sort 3.8 protein and nucleic acid folding: domain swapping in proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7152442/
http://dx.doi.org/10.1016/B978-0-12-374920-8.00309-X
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