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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
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.
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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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