SWISS-MODEL: homology modelling of protein structures and complexes
Author(s) -
Andrew Waterhouse,
Martino Bertoni,
Stefan Bienert,
Gabriel Studer,
Gerardo Tauriello,
Rafal Gumienny,
Florian Heer,
Tjaart de Beer,
Christine Rempfer,
Lorenza Bordoli,
Rosalba Lepore,
Torsten Schwede
Publication year - 2018
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gky427
Subject(s) - homology modeling , workflow , biology , homology (biology) , computational biology , visualization , computer science , bioinformatics , data mining , amino acid , genetics , database , biochemistry , enzyme
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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