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PlaPPISite: a comprehensive resource for plant protein-protein interaction sites

BACKGROUND: Protein-protein interactions (PPIs) play very important roles in diverse biological processes. Experimentally validated or predicted PPI data have become increasingly available in diverse plant species. To further explore the biological functions of PPIs, understanding the interaction de...

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Autores principales: Yang, Xiaodi, Yang, Shiping, Qi, Huan, Wang, Tianpeng, Li, Hong, Zhang, Ziding
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7006421/
https://www.ncbi.nlm.nih.gov/pubmed/32028878
http://dx.doi.org/10.1186/s12870-020-2254-4
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author Yang, Xiaodi
Yang, Shiping
Qi, Huan
Wang, Tianpeng
Li, Hong
Zhang, Ziding
author_facet Yang, Xiaodi
Yang, Shiping
Qi, Huan
Wang, Tianpeng
Li, Hong
Zhang, Ziding
author_sort Yang, Xiaodi
collection PubMed
description BACKGROUND: Protein-protein interactions (PPIs) play very important roles in diverse biological processes. Experimentally validated or predicted PPI data have become increasingly available in diverse plant species. To further explore the biological functions of PPIs, understanding the interaction details of plant PPIs (e.g., the 3D structural contexts of interaction sites) is necessary. By integrating bioinformatics algorithms, interaction details can be annotated at different levels and then compiled into user-friendly databases. In our previous study, we developed AraPPISite, which aimed to provide interaction site information for PPIs in the model plant Arabidopsis thaliana. Considering that the application of AraPPISite is limited to one species, it is very natural that AraPPISite should be evolved into a new database that can provide interaction details of PPIs in multiple plants. DESCRIPTION: PlaPPISite (http://zzdlab.com/plappisite/index.php) is a comprehensive, high-coverage and interaction details-oriented database for 13 plant interactomes. In addition to collecting 121 experimentally verified structures of protein complexes, the complex structures of experimental/predicted PPIs in the 13 plants were also constructed, and the corresponding interaction sites were annotated. For the PPIs whose 3D structures could not be modelled, the associated domain-domain interactions (DDIs) and domain-motif interactions (DMIs) were inferred. To facilitate the reliability assessment of predicted PPIs, the source species of interolog templates, GO annotations, subcellular localizations and gene expression similarities are also provided. JavaScript packages were employed to visualize structures of protein complexes, protein interaction sites and protein interaction networks. We also developed an online tool for homology modelling and protein interaction site annotation of protein complexes. All data contained in PlaPPISite are also freely available on the Download page. CONCLUSION: PlaPPISite provides the plant research community with an easy-to-use and comprehensive data resource for the search and analysis of protein interaction details from the 13 important plant species.
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spelling pubmed-70064212020-02-13 PlaPPISite: a comprehensive resource for plant protein-protein interaction sites Yang, Xiaodi Yang, Shiping Qi, Huan Wang, Tianpeng Li, Hong Zhang, Ziding BMC Plant Biol Database BACKGROUND: Protein-protein interactions (PPIs) play very important roles in diverse biological processes. Experimentally validated or predicted PPI data have become increasingly available in diverse plant species. To further explore the biological functions of PPIs, understanding the interaction details of plant PPIs (e.g., the 3D structural contexts of interaction sites) is necessary. By integrating bioinformatics algorithms, interaction details can be annotated at different levels and then compiled into user-friendly databases. In our previous study, we developed AraPPISite, which aimed to provide interaction site information for PPIs in the model plant Arabidopsis thaliana. Considering that the application of AraPPISite is limited to one species, it is very natural that AraPPISite should be evolved into a new database that can provide interaction details of PPIs in multiple plants. DESCRIPTION: PlaPPISite (http://zzdlab.com/plappisite/index.php) is a comprehensive, high-coverage and interaction details-oriented database for 13 plant interactomes. In addition to collecting 121 experimentally verified structures of protein complexes, the complex structures of experimental/predicted PPIs in the 13 plants were also constructed, and the corresponding interaction sites were annotated. For the PPIs whose 3D structures could not be modelled, the associated domain-domain interactions (DDIs) and domain-motif interactions (DMIs) were inferred. To facilitate the reliability assessment of predicted PPIs, the source species of interolog templates, GO annotations, subcellular localizations and gene expression similarities are also provided. JavaScript packages were employed to visualize structures of protein complexes, protein interaction sites and protein interaction networks. We also developed an online tool for homology modelling and protein interaction site annotation of protein complexes. All data contained in PlaPPISite are also freely available on the Download page. CONCLUSION: PlaPPISite provides the plant research community with an easy-to-use and comprehensive data resource for the search and analysis of protein interaction details from the 13 important plant species. BioMed Central 2020-02-06 /pmc/articles/PMC7006421/ /pubmed/32028878 http://dx.doi.org/10.1186/s12870-020-2254-4 Text en © The Author(s). 2020 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Database
Yang, Xiaodi
Yang, Shiping
Qi, Huan
Wang, Tianpeng
Li, Hong
Zhang, Ziding
PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title_full PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title_fullStr PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title_full_unstemmed PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title_short PlaPPISite: a comprehensive resource for plant protein-protein interaction sites
title_sort plappisite: a comprehensive resource for plant protein-protein interaction sites
topic Database
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7006421/
https://www.ncbi.nlm.nih.gov/pubmed/32028878
http://dx.doi.org/10.1186/s12870-020-2254-4
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AT lihong plappisiteacomprehensiveresourceforplantproteinproteininteractionsites
AT zhangziding plappisiteacomprehensiveresourceforplantproteinproteininteractionsites