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SWISS-MODEL: homology modelling of protein structures and complexes

Open access
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·2018·Nucleic Acids Research

Abstract

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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Metadata

Authors
Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T. A. P., Rempfer, C., Bordoli, L., Lepore, R., & Schwede, T.
Venue
Nucleic Acids Research
Published
2018-05-21
Volume
46
Issue
W1
Pages
W296-W303
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2804822363
Cited by
13,067
References
11
FWCI
345.61
Type
journal article
Language
en
Open access
gold

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