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SWISS-MODEL: homology modelling of protein structures and complexes
Homology modelling has matured into an important technique in structural biology, significantly contributing to narrowing the gap between known protein sequences and experimentally determined structures. Fully automated workflows and servers simplify and streamline the homology modelling process, al...
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/PMC6030848/ https://www.ncbi.nlm.nih.gov/pubmed/29788355 http://dx.doi.org/10.1093/nar/gky427 |
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author | Waterhouse, Andrew Bertoni, Martino Bienert, Stefan Studer, Gabriel Tauriello, Gerardo Gumienny, Rafal Heer, Florian T de Beer, Tjaart A P Rempfer, Christine Bordoli, Lorenza Lepore, Rosalba Schwede, Torsten |
author_facet | Waterhouse, Andrew Bertoni, Martino Bienert, Stefan Studer, Gabriel Tauriello, Gerardo Gumienny, Rafal Heer, Florian T de Beer, Tjaart A P Rempfer, Christine Bordoli, Lorenza Lepore, Rosalba Schwede, Torsten |
author_sort | Waterhouse, Andrew |
collection | PubMed |
description | Homology modelling has matured into an important technique in structural biology, significantly contributing to narrowing the gap between known protein sequences and experimentally determined structures. Fully automated workflows and servers simplify and streamline the homology modelling process, also allowing users without a specific computational expertise to generate reliable protein models and have easy access to modelling results, their visualization and interpretation. Here, we present an update to the SWISS-MODEL server, which pioneered the field of automated modelling 25 years ago and been continuously further developed. Recently, its functionality has been extended to the modelling of homo- and heteromeric complexes. Starting from the amino acid sequences of the interacting proteins, both the stoichiometry and the overall structure of the complex are inferred by homology modelling. Other major improvements include the implementation of a new modelling engine, ProMod3 and the introduction a new local model quality estimation method, QMEANDisCo. SWISS-MODEL is freely available at https://swissmodel.expasy.org. |
format | Online Article Text |
id | pubmed-6030848 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-60308482018-07-10 SWISS-MODEL: homology modelling of protein structures and complexes Waterhouse, Andrew Bertoni, Martino Bienert, Stefan Studer, Gabriel Tauriello, Gerardo Gumienny, Rafal Heer, Florian T de Beer, Tjaart A P Rempfer, Christine Bordoli, Lorenza Lepore, Rosalba Schwede, Torsten Nucleic Acids Res Web Server Issue Homology modelling has matured into an important technique in structural biology, significantly contributing to narrowing the gap between known protein sequences and experimentally determined structures. Fully automated workflows and servers simplify and streamline the homology modelling process, also allowing users without a specific computational expertise to generate reliable protein models and have easy access to modelling results, their visualization and interpretation. Here, we present an update to the SWISS-MODEL server, which pioneered the field of automated modelling 25 years ago and been continuously further developed. Recently, its functionality has been extended to the modelling of homo- and heteromeric complexes. Starting from the amino acid sequences of the interacting proteins, both the stoichiometry and the overall structure of the complex are inferred by homology modelling. Other major improvements include the implementation of a new modelling engine, ProMod3 and the introduction a new local model quality estimation method, QMEANDisCo. SWISS-MODEL is freely available at https://swissmodel.expasy.org. Oxford University Press 2018-07-02 2018-05-21 /pmc/articles/PMC6030848/ /pubmed/29788355 http://dx.doi.org/10.1093/nar/gky427 Text en © The Author(s) 2018. 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 Waterhouse, Andrew Bertoni, Martino Bienert, Stefan Studer, Gabriel Tauriello, Gerardo Gumienny, Rafal Heer, Florian T de Beer, Tjaart A P Rempfer, Christine Bordoli, Lorenza Lepore, Rosalba Schwede, Torsten SWISS-MODEL: homology modelling of protein structures and complexes |
title | SWISS-MODEL: homology modelling of protein structures and complexes |
title_full | SWISS-MODEL: homology modelling of protein structures and complexes |
title_fullStr | SWISS-MODEL: homology modelling of protein structures and complexes |
title_full_unstemmed | SWISS-MODEL: homology modelling of protein structures and complexes |
title_short | SWISS-MODEL: homology modelling of protein structures and complexes |
title_sort | swiss-model: homology modelling of protein structures and complexes |
topic | Web Server Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6030848/ https://www.ncbi.nlm.nih.gov/pubmed/29788355 http://dx.doi.org/10.1093/nar/gky427 |
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