Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin

The plakin repeat domain is a distinctive hallmark of the plakin superfamily of proteins, which are found within all epithelial tissues. Plakin repeat domains mediate the interactions of these proteins with the cell cytoskeleton and are critical for the maintenance of tissue integrity. Despite their...

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Autores principales: Jeeves, Mark, Fogl, Claudia, Al-Jassar, Caezar, Chidgey, Martyn, Overduin, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4788679/
https://www.ncbi.nlm.nih.gov/pubmed/26590577
http://dx.doi.org/10.1007/s12104-015-9659-2
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author Jeeves, Mark
Fogl, Claudia
Al-Jassar, Caezar
Chidgey, Martyn
Overduin, Michael
author_facet Jeeves, Mark
Fogl, Claudia
Al-Jassar, Caezar
Chidgey, Martyn
Overduin, Michael
author_sort Jeeves, Mark
collection PubMed
description The plakin repeat domain is a distinctive hallmark of the plakin superfamily of proteins, which are found within all epithelial tissues. Plakin repeat domains mediate the interactions of these proteins with the cell cytoskeleton and are critical for the maintenance of tissue integrity. Despite their biological importance, no solution state resonance assignments are available for any homologue. Here we report the essentially complete (1)H, (13)C and (15)N backbone chemical shift assignments of the singular 22 kDa plakin repeat domain of human envoplakin, providing the means to investigate its interactions with ligands including intermediate filaments.
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spelling pubmed-47886792016-04-09 Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin Jeeves, Mark Fogl, Claudia Al-Jassar, Caezar Chidgey, Martyn Overduin, Michael Biomol NMR Assign Article The plakin repeat domain is a distinctive hallmark of the plakin superfamily of proteins, which are found within all epithelial tissues. Plakin repeat domains mediate the interactions of these proteins with the cell cytoskeleton and are critical for the maintenance of tissue integrity. Despite their biological importance, no solution state resonance assignments are available for any homologue. Here we report the essentially complete (1)H, (13)C and (15)N backbone chemical shift assignments of the singular 22 kDa plakin repeat domain of human envoplakin, providing the means to investigate its interactions with ligands including intermediate filaments. Springer Netherlands 2015-11-21 2016 /pmc/articles/PMC4788679/ /pubmed/26590577 http://dx.doi.org/10.1007/s12104-015-9659-2 Text en © The Author(s) 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Jeeves, Mark
Fogl, Claudia
Al-Jassar, Caezar
Chidgey, Martyn
Overduin, Michael
Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title_full Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title_fullStr Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title_full_unstemmed Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title_short Sequence-specific (1)H, (13)C and (15)N backbone resonance assignments of the plakin repeat domain of human envoplakin
title_sort sequence-specific (1)h, (13)c and (15)n backbone resonance assignments of the plakin repeat domain of human envoplakin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4788679/
https://www.ncbi.nlm.nih.gov/pubmed/26590577
http://dx.doi.org/10.1007/s12104-015-9659-2
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