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Intercalative DNA binding of the marine anticancer drug variolin B
Variolin B is a rare marine alkaloid that showed promising anti-cancer activity soon after its isolation. It acts as a cyclin-dependent kinase inhibitor, although the precise mechanism through which it exerts the cytotoxic effects is still unknown. The crystal structure of a variolin B bound to a DN...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209663/ https://www.ncbi.nlm.nih.gov/pubmed/28051169 http://dx.doi.org/10.1038/srep39680 |
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author | Canals, Albert Arribas-Bosacoma, Raquel Albericio, Fernando Álvarez, Mercedes Aymamí, Joan Coll, Miquel |
author_facet | Canals, Albert Arribas-Bosacoma, Raquel Albericio, Fernando Álvarez, Mercedes Aymamí, Joan Coll, Miquel |
author_sort | Canals, Albert |
collection | PubMed |
description | Variolin B is a rare marine alkaloid that showed promising anti-cancer activity soon after its isolation. It acts as a cyclin-dependent kinase inhibitor, although the precise mechanism through which it exerts the cytotoxic effects is still unknown. The crystal structure of a variolin B bound to a DNA forming a pseudo-Holliday junction shows that this compound can also contribute, through intercalative binding, to either the formation or stabilization of multi-stranded DNA forms. |
format | Online Article Text |
id | pubmed-5209663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52096632017-01-04 Intercalative DNA binding of the marine anticancer drug variolin B Canals, Albert Arribas-Bosacoma, Raquel Albericio, Fernando Álvarez, Mercedes Aymamí, Joan Coll, Miquel Sci Rep Article Variolin B is a rare marine alkaloid that showed promising anti-cancer activity soon after its isolation. It acts as a cyclin-dependent kinase inhibitor, although the precise mechanism through which it exerts the cytotoxic effects is still unknown. The crystal structure of a variolin B bound to a DNA forming a pseudo-Holliday junction shows that this compound can also contribute, through intercalative binding, to either the formation or stabilization of multi-stranded DNA forms. Nature Publishing Group 2017-01-04 /pmc/articles/PMC5209663/ /pubmed/28051169 http://dx.doi.org/10.1038/srep39680 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Canals, Albert Arribas-Bosacoma, Raquel Albericio, Fernando Álvarez, Mercedes Aymamí, Joan Coll, Miquel Intercalative DNA binding of the marine anticancer drug variolin B |
title | Intercalative DNA binding of the marine anticancer drug variolin B |
title_full | Intercalative DNA binding of the marine anticancer drug variolin B |
title_fullStr | Intercalative DNA binding of the marine anticancer drug variolin B |
title_full_unstemmed | Intercalative DNA binding of the marine anticancer drug variolin B |
title_short | Intercalative DNA binding of the marine anticancer drug variolin B |
title_sort | intercalative dna binding of the marine anticancer drug variolin b |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5209663/ https://www.ncbi.nlm.nih.gov/pubmed/28051169 http://dx.doi.org/10.1038/srep39680 |
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