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Troponin structure and function: a view of recent progress

The molecular mechanism by which Ca(2+) binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a ch...

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Detalles Bibliográficos
Autores principales: Marston, Steven, Zamora, Juan Eiros
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7109197/
https://www.ncbi.nlm.nih.gov/pubmed/31030382
http://dx.doi.org/10.1007/s10974-019-09513-1
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author Marston, Steven
Zamora, Juan Eiros
author_facet Marston, Steven
Zamora, Juan Eiros
author_sort Marston, Steven
collection PubMed
description The molecular mechanism by which Ca(2+) binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca(2+), phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies.
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spelling pubmed-71091972020-04-06 Troponin structure and function: a view of recent progress Marston, Steven Zamora, Juan Eiros J Muscle Res Cell Motil Article The molecular mechanism by which Ca(2+) binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca(2+), phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies. Springer International Publishing 2019-04-27 2020 /pmc/articles/PMC7109197/ /pubmed/31030382 http://dx.doi.org/10.1007/s10974-019-09513-1 Text en © The Author(s) 2019 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
Marston, Steven
Zamora, Juan Eiros
Troponin structure and function: a view of recent progress
title Troponin structure and function: a view of recent progress
title_full Troponin structure and function: a view of recent progress
title_fullStr Troponin structure and function: a view of recent progress
title_full_unstemmed Troponin structure and function: a view of recent progress
title_short Troponin structure and function: a view of recent progress
title_sort troponin structure and function: a view of recent progress
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7109197/
https://www.ncbi.nlm.nih.gov/pubmed/31030382
http://dx.doi.org/10.1007/s10974-019-09513-1
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