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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2019
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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. |
format | Online Article Text |
id | pubmed-7109197 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT marstonsteven troponinstructureandfunctionaviewofrecentprogress AT zamorajuaneiros troponinstructureandfunctionaviewofrecentprogress |