ArticlePlant molecular biology2016
AraPPISite: a database of fine-grained protein-protein interaction site annotations for Arabidopsis thaliana.
Article in Plant molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Using PlaPPISite to Predict and Analyze Plant Protein-Protein Interaction Sites.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Evolution of 14-3-3 Proteins in Angiosperm Plants: Recurring Gene Duplication and Loss.Plants (Basel, Switzerland) · 2021Article
- Network-based analysis of virulence factors for uncovering Aeromonas veronii pathogenesis.BMC microbiology · 2021Article
- PlaPPISite: a comprehensive resource for plant protein-protein interaction sites.BMC plant biology · 2020Article
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Authors and funding
5 authors.
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Abstract
Knowledge about protein interaction sites provides detailed information of protein-protein interactions (PPIs). To date, nearly 20,000 of PPIs from Arabidopsis thaliana have been identified. Nevertheless, the interaction site information has been largely missed by previously published PPI databases. Here, AraPPISite, a database that presents fine-grained interaction details for A. thaliana PPIs is established. First, the experimentally determined 3D structures of 27 A. thaliana PPIs are collected from the Protein Data Bank database and the predicted 3D structures of 3023 A. thaliana PPIs are modeled by using two well-established template-based docking methods. For each experimental/predicted complex structure, AraPPISite not only provides an interactive user interface for browsing interaction sites, but also lists detailed evolutionary and physicochemical properties of these sites. Second, AraPPISite assigns domain-domain interactions or domain-motif interactions to 4286 PPIs whose 3D structures cannot be modeled. In this case, users can easily query protein interaction regions at the sequence level. AraPPISite is a free and user-friendly database, which does not require user registration or any configuration on local machines. We anticipate AraPPISite can serve as a helpful database resource for the users with less experience in structural biology or protein bioinformatics to probe the details of PPIs, and thus accelerate the studies of plant genetics and functional genomics. AraPPISite is available at http://systbio.cau.edu.cn/arappisite/index.html .
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