FATCAT 2.0: towards a better understanding of the structural diversity of proteins

FATCAT 2.0 server (http://fatcat.godziklab.org/), provides access to a flexible protein structure alignment algorithm developed in our group. In such an alignment, rotations and translations between elements in the structure are allowed to minimize the overall root mean square deviation (RMSD) betwe...

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Detalles Bibliográficos
Autores principales: Li, Zhanwen, Jaroszewski, Lukasz, Iyer, Mallika, Sedova, Mayya, Godzik, Adam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Web Server Issue
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7319568/
https://www.ncbi.nlm.nih.gov/pubmed/32469061
http://dx.doi.org/10.1093/nar/gkaa443
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author Li, Zhanwen
Jaroszewski, Lukasz
Iyer, Mallika
Sedova, Mayya
Godzik, Adam
author_facet Li, Zhanwen
Jaroszewski, Lukasz
Iyer, Mallika
Sedova, Mayya
Godzik, Adam
author_sort Li, Zhanwen
collection PubMed
description FATCAT 2.0 server (http://fatcat.godziklab.org/), provides access to a flexible protein structure alignment algorithm developed in our group. In such an alignment, rotations and translations between elements in the structure are allowed to minimize the overall root mean square deviation (RMSD) between the compared structures. This allows to effectively compare protein structures even if they underwent structural rearrangements in different functional forms, different crystallization conditions or as a result of mutations. The major update for the server introduces a new graphical interface, much faster database searches and several new options for visualization of the structural differences between proteins
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spelling pubmed-73195682020-07-01 FATCAT 2.0: towards a better understanding of the structural diversity of proteins Li, Zhanwen Jaroszewski, Lukasz Iyer, Mallika Sedova, Mayya Godzik, Adam Nucleic Acids Res Web Server Issue FATCAT 2.0 server (http://fatcat.godziklab.org/), provides access to a flexible protein structure alignment algorithm developed in our group. In such an alignment, rotations and translations between elements in the structure are allowed to minimize the overall root mean square deviation (RMSD) between the compared structures. This allows to effectively compare protein structures even if they underwent structural rearrangements in different functional forms, different crystallization conditions or as a result of mutations. The major update for the server introduces a new graphical interface, much faster database searches and several new options for visualization of the structural differences between proteins Oxford University Press 2020-07-02 2020-05-29 /pmc/articles/PMC7319568/ /pubmed/32469061 http://dx.doi.org/10.1093/nar/gkaa443 Text en © The Author(s) 2020. 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
Li, Zhanwen
Jaroszewski, Lukasz
Iyer, Mallika
Sedova, Mayya
Godzik, Adam
FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title_full FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title_fullStr FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title_full_unstemmed FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title_short FATCAT 2.0: towards a better understanding of the structural diversity of proteins
title_sort fatcat 2.0: towards a better understanding of the structural diversity of proteins
topic Web Server Issue
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7319568/
https://www.ncbi.nlm.nih.gov/pubmed/32469061
http://dx.doi.org/10.1093/nar/gkaa443
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