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I-COMS: Interprotein-COrrelated Mutations Server
Interprotein contact prediction using multiple sequence alignments (MSAs) is a useful approach to help detect protein–protein interfaces. Different computational methods have been developed in recent years as an approximation to solve this problem. However, as there are discrepancies in the results...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489276/ https://www.ncbi.nlm.nih.gov/pubmed/26032772 http://dx.doi.org/10.1093/nar/gkv572 |
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author | Iserte, Javier Simonetti, Franco L. Zea, Diego J. Teppa, Elin Marino-Buslje, Cristina |
author_facet | Iserte, Javier Simonetti, Franco L. Zea, Diego J. Teppa, Elin Marino-Buslje, Cristina |
author_sort | Iserte, Javier |
collection | PubMed |
description | Interprotein contact prediction using multiple sequence alignments (MSAs) is a useful approach to help detect protein–protein interfaces. Different computational methods have been developed in recent years as an approximation to solve this problem. However, as there are discrepancies in the results provided by them, there is still no consensus on which is the best performing methodology. To address this problem, I-COMS (interprotein COrrelated Mutations Server) is presented. I-COMS allows to estimate covariation between residues of different proteins by four different covariation methods. It provides a graphical and interactive output that helps compare results obtained using different methods. I-COMS automatically builds the required MSA for the calculation and produces a rich visualization of either intraprotein and/or interprotein covariating positions in a circos representation. Furthermore, comparison between any two methods is available as well as the overlap between any or all four methodologies. In addition, as a complementary source of information, a matrix visualization of the corresponding scores is made available and the density plot distribution of the inter, intra and inter+intra scores are calculated. Finally, all the results can be downloaded (including MSAs, scores and graphics) for comparison and visualization and/or for further analysis. |
format | Online Article Text |
id | pubmed-4489276 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-44892762015-07-07 I-COMS: Interprotein-COrrelated Mutations Server Iserte, Javier Simonetti, Franco L. Zea, Diego J. Teppa, Elin Marino-Buslje, Cristina Nucleic Acids Res Web Server issue Interprotein contact prediction using multiple sequence alignments (MSAs) is a useful approach to help detect protein–protein interfaces. Different computational methods have been developed in recent years as an approximation to solve this problem. However, as there are discrepancies in the results provided by them, there is still no consensus on which is the best performing methodology. To address this problem, I-COMS (interprotein COrrelated Mutations Server) is presented. I-COMS allows to estimate covariation between residues of different proteins by four different covariation methods. It provides a graphical and interactive output that helps compare results obtained using different methods. I-COMS automatically builds the required MSA for the calculation and produces a rich visualization of either intraprotein and/or interprotein covariating positions in a circos representation. Furthermore, comparison between any two methods is available as well as the overlap between any or all four methodologies. In addition, as a complementary source of information, a matrix visualization of the corresponding scores is made available and the density plot distribution of the inter, intra and inter+intra scores are calculated. Finally, all the results can be downloaded (including MSAs, scores and graphics) for comparison and visualization and/or for further analysis. Oxford University Press 2015-07-01 2015-06-01 /pmc/articles/PMC4489276/ /pubmed/26032772 http://dx.doi.org/10.1093/nar/gkv572 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. 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 | Web Server issue Iserte, Javier Simonetti, Franco L. Zea, Diego J. Teppa, Elin Marino-Buslje, Cristina I-COMS: Interprotein-COrrelated Mutations Server |
title | I-COMS: Interprotein-COrrelated Mutations Server |
title_full | I-COMS: Interprotein-COrrelated Mutations Server |
title_fullStr | I-COMS: Interprotein-COrrelated Mutations Server |
title_full_unstemmed | I-COMS: Interprotein-COrrelated Mutations Server |
title_short | I-COMS: Interprotein-COrrelated Mutations Server |
title_sort | i-coms: interprotein-correlated mutations server |
topic | Web Server issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4489276/ https://www.ncbi.nlm.nih.gov/pubmed/26032772 http://dx.doi.org/10.1093/nar/gkv572 |
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