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MDAT- Aligning multiple domain arrangements
BACKGROUND: Proteins are composed of domains, protein segments that fold independently from the rest of the protein and have a specific function. During evolution the arrangement of domains can change: domains are gained, lost or their order is rearranged. To facilitate the analysis of these changes...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384290/ https://www.ncbi.nlm.nih.gov/pubmed/25626688 http://dx.doi.org/10.1186/s12859-014-0442-7 |
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author | Kemena, Carsten Bitard-Feildel, Tristan Bornberg-Bauer, Erich |
author_facet | Kemena, Carsten Bitard-Feildel, Tristan Bornberg-Bauer, Erich |
author_sort | Kemena, Carsten |
collection | PubMed |
description | BACKGROUND: Proteins are composed of domains, protein segments that fold independently from the rest of the protein and have a specific function. During evolution the arrangement of domains can change: domains are gained, lost or their order is rearranged. To facilitate the analysis of these changes we propose the use of multiple domain alignments. RESULTS: We developed an alignment program, called MDAT, which aligns multiple domain arrangements. MDAT extends earlier programs which perform pairwise alignments of domain arrangements. MDAT uses a domain similarity matrix to score domain pairs and aligns the domain arrangements using a consistency supported progressive alignment method. CONCLUSION: MDAT will be useful for analysing changes in domain arrangements within and between protein families and will thus provide valuable insights into the evolution of proteins and their domains. MDAT is coded in C++, and the source code is freely available for download at http://www.bornberglab.org/pages/mdat. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12859-014-0442-7) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4384290 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-43842902015-04-04 MDAT- Aligning multiple domain arrangements Kemena, Carsten Bitard-Feildel, Tristan Bornberg-Bauer, Erich BMC Bioinformatics Methodology Article BACKGROUND: Proteins are composed of domains, protein segments that fold independently from the rest of the protein and have a specific function. During evolution the arrangement of domains can change: domains are gained, lost or their order is rearranged. To facilitate the analysis of these changes we propose the use of multiple domain alignments. RESULTS: We developed an alignment program, called MDAT, which aligns multiple domain arrangements. MDAT extends earlier programs which perform pairwise alignments of domain arrangements. MDAT uses a domain similarity matrix to score domain pairs and aligns the domain arrangements using a consistency supported progressive alignment method. CONCLUSION: MDAT will be useful for analysing changes in domain arrangements within and between protein families and will thus provide valuable insights into the evolution of proteins and their domains. MDAT is coded in C++, and the source code is freely available for download at http://www.bornberglab.org/pages/mdat. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12859-014-0442-7) contains supplementary material, which is available to authorized users. BioMed Central 2015-01-28 /pmc/articles/PMC4384290/ /pubmed/25626688 http://dx.doi.org/10.1186/s12859-014-0442-7 Text en © Kemena et al.; licensee BioMed Central. 2015 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 use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Methodology Article Kemena, Carsten Bitard-Feildel, Tristan Bornberg-Bauer, Erich MDAT- Aligning multiple domain arrangements |
title | MDAT- Aligning multiple domain arrangements |
title_full | MDAT- Aligning multiple domain arrangements |
title_fullStr | MDAT- Aligning multiple domain arrangements |
title_full_unstemmed | MDAT- Aligning multiple domain arrangements |
title_short | MDAT- Aligning multiple domain arrangements |
title_sort | mdat- aligning multiple domain arrangements |
topic | Methodology Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384290/ https://www.ncbi.nlm.nih.gov/pubmed/25626688 http://dx.doi.org/10.1186/s12859-014-0442-7 |
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