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HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry
A major subclass of protein–protein interactions is formed by homo-oligomers with certain symmetry. Therefore, computational modeling of the symmetric protein complexes is important for understanding the molecular mechanism of related biological processes. Although several symmetric docking algorith...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6030965/ https://www.ncbi.nlm.nih.gov/pubmed/29846641 http://dx.doi.org/10.1093/nar/gky398 |
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author | Yan, Yumeng Tao, Huanyu Huang, Sheng-You |
author_facet | Yan, Yumeng Tao, Huanyu Huang, Sheng-You |
author_sort | Yan, Yumeng |
collection | PubMed |
description | A major subclass of protein–protein interactions is formed by homo-oligomers with certain symmetry. Therefore, computational modeling of the symmetric protein complexes is important for understanding the molecular mechanism of related biological processes. Although several symmetric docking algorithms have been developed for Cn symmetry, few docking servers have been proposed for Dn symmetry. Here, we present HSYMDOCK, a web server of our hierarchical symmetric docking algorithm that supports both Cn and Dn symmetry. The HSYMDOCK server was extensively evaluated on three benchmarks of symmetric protein complexes, including the 20 CASP11–CAPRI30 homo-oligomer targets, the symmetric docking benchmark of 213 Cn targets and 35 Dn targets, and a nonredundant test set of 55 transmembrane proteins. It was shown that HSYMDOCK obtained a significantly better performance than other similar docking algorithms. The server supports both sequence and structure inputs for the monomer/subunit. Users have an option to provide the symmetry type of the complex, or the server can predict the symmetry type automatically. The docking process is fast and on average consumes 10∼20 min for a docking job. The HSYMDOCK web server is available at http://huanglab.phys.hust.edu.cn/hsymdock/. |
format | Online Article Text |
id | pubmed-6030965 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-60309652018-07-10 HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry Yan, Yumeng Tao, Huanyu Huang, Sheng-You Nucleic Acids Res Web Server Issue A major subclass of protein–protein interactions is formed by homo-oligomers with certain symmetry. Therefore, computational modeling of the symmetric protein complexes is important for understanding the molecular mechanism of related biological processes. Although several symmetric docking algorithms have been developed for Cn symmetry, few docking servers have been proposed for Dn symmetry. Here, we present HSYMDOCK, a web server of our hierarchical symmetric docking algorithm that supports both Cn and Dn symmetry. The HSYMDOCK server was extensively evaluated on three benchmarks of symmetric protein complexes, including the 20 CASP11–CAPRI30 homo-oligomer targets, the symmetric docking benchmark of 213 Cn targets and 35 Dn targets, and a nonredundant test set of 55 transmembrane proteins. It was shown that HSYMDOCK obtained a significantly better performance than other similar docking algorithms. The server supports both sequence and structure inputs for the monomer/subunit. Users have an option to provide the symmetry type of the complex, or the server can predict the symmetry type automatically. The docking process is fast and on average consumes 10∼20 min for a docking job. The HSYMDOCK web server is available at http://huanglab.phys.hust.edu.cn/hsymdock/. Oxford University Press 2018-07-02 2018-05-26 /pmc/articles/PMC6030965/ /pubmed/29846641 http://dx.doi.org/10.1093/nar/gky398 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Web Server Issue Yan, Yumeng Tao, Huanyu Huang, Sheng-You HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title | HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title_full | HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title_fullStr | HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title_full_unstemmed | HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title_short | HSYMDOCK: a docking web server for predicting the structure of protein homo-oligomers with Cn or Dn symmetry |
title_sort | hsymdock: a docking web server for predicting the structure of protein homo-oligomers with cn or dn symmetry |
topic | Web Server Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6030965/ https://www.ncbi.nlm.nih.gov/pubmed/29846641 http://dx.doi.org/10.1093/nar/gky398 |
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