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CCProf: exploring conformational change profile of proteins

In many biological processes, proteins have important interactions with various molecules such as proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the...

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Detalles Bibliográficos
Autores principales: Chang, Che-Wei, Chou, Chai-Wei, Chang, Darby Tien-Hao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4808249/
https://www.ncbi.nlm.nih.gov/pubmed/27016699
http://dx.doi.org/10.1093/database/baw029
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author Chang, Che-Wei
Chou, Chai-Wei
Chang, Darby Tien-Hao
author_facet Chang, Che-Wei
Chou, Chai-Wei
Chang, Darby Tien-Hao
author_sort Chang, Che-Wei
collection PubMed
description In many biological processes, proteins have important interactions with various molecules such as proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the CCProf platform, which provides conformational changes of entire proteins, named conformational change profile (CCP) in the context. CCProf aims to be a platform where users can study potential causes of novel conformational changes. It provides 10 biological features, including conformational change, potential binding target site, secondary structure, conservation, disorder propensity, hydropathy propensity, sequence domain, structural domain, phosphorylation site and catalytic site. All these information are integrated into a well-aligned view, so that researchers can capture important relevance between different biological features visually. The CCProf contains 986 187 protein structure pairs for 3123 proteins. In addition, CCProf provides a 3D view in which users can see the protein structures before and after conformational changes as well as binding targets that induce conformational changes. All information (e.g. CCP, binding targets and protein structures) shown in CCProf, including intermediate data are available for download to expedite further analyses. Database URL: http://zoro.ee.ncku.edu.tw/ccprof/
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spelling pubmed-48082492016-03-29 CCProf: exploring conformational change profile of proteins Chang, Che-Wei Chou, Chai-Wei Chang, Darby Tien-Hao Database (Oxford) Original Article In many biological processes, proteins have important interactions with various molecules such as proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the CCProf platform, which provides conformational changes of entire proteins, named conformational change profile (CCP) in the context. CCProf aims to be a platform where users can study potential causes of novel conformational changes. It provides 10 biological features, including conformational change, potential binding target site, secondary structure, conservation, disorder propensity, hydropathy propensity, sequence domain, structural domain, phosphorylation site and catalytic site. All these information are integrated into a well-aligned view, so that researchers can capture important relevance between different biological features visually. The CCProf contains 986 187 protein structure pairs for 3123 proteins. In addition, CCProf provides a 3D view in which users can see the protein structures before and after conformational changes as well as binding targets that induce conformational changes. All information (e.g. CCP, binding targets and protein structures) shown in CCProf, including intermediate data are available for download to expedite further analyses. Database URL: http://zoro.ee.ncku.edu.tw/ccprof/ Oxford University Press 2016-03-25 /pmc/articles/PMC4808249/ /pubmed/27016699 http://dx.doi.org/10.1093/database/baw029 Text en © The Author(s) 2016. Published by Oxford University Press. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Chang, Che-Wei
Chou, Chai-Wei
Chang, Darby Tien-Hao
CCProf: exploring conformational change profile of proteins
title CCProf: exploring conformational change profile of proteins
title_full CCProf: exploring conformational change profile of proteins
title_fullStr CCProf: exploring conformational change profile of proteins
title_full_unstemmed CCProf: exploring conformational change profile of proteins
title_short CCProf: exploring conformational change profile of proteins
title_sort ccprof: exploring conformational change profile of proteins
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4808249/
https://www.ncbi.nlm.nih.gov/pubmed/27016699
http://dx.doi.org/10.1093/database/baw029
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