DIBS: a repository of disordered binding sites mediating interactions with ordered proteins
By É. Schád, Erzsébet Fichó, Rita Pancsa, István Simon, Zsuzsanna Dosztányi, Bálint Mészáros. 2017
83 citations recorded by the source corpus.
Motivation Intrinsically Disordered Proteins (IDPs) mediate crucial protein‐protein interactions, most notably in signaling and regulation. As their importance is increasingly recognized, the detailed analyses of specific IDP interactions opened up new opportunities for therapeutic targeting. Yet, large scale information about IDP‐mediated interactions in structural and functional details are lacking, hindering the understanding of the mechanisms underlying this distinct binding mode. Results Here, we present DIBS, the first comprehensive, curated collection of complexes between IDPs and ordered proteins. DIBS not only describes by far the highest number of cases, it also provides the dissociation constants of their interactions, as well as the description of potential post‐translational modifications modulating the binding strength and linear motifs involved in the binding. Together with the wide range of structural and functional annotations, DIBS will provide the cornerstone for structural and functional studies of IDP complexes. Availability and implementation DIBS is freely accessible at http://dibs.enzim.ttk.mta.hu/. The DIBS application is hosted by Apache web server and was implemented in PHP. To enrich querying features and to enhance backend performance a MySQL database was also created.
Subfields: Molecular Biology
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In Molecular Biology
- Zsuzsanna Dosztányi
- Gábor Erdös
- Bálint Mészáros
- Vladimir N Uversky
- Michele Vendruscolo
- Damiano Piovesan
- Silvio C. E. Tosatto
- Lukasz Kurgan
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “In this regard, a major new development was the launch of the DIBS database, which collects protein complexes where one partner was shown experimentally to be both disordered in isolation and being involved in disorder-to-order transition (36).”
- MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “Overview of databases integrated into MobiDB 3.0 Database Type Comment URL UniProt Curated Disorder http://www.uniprot.org/ DisProt Curated Disorder http://www.disprot.org/ FuzDB Curated Disorder http://protdyn-database.org/ ELM Curated LIPs http://elm.eu.org/ MFIB Curated LIPs http://mfib.enzim.ttk”
- Analyzing Protein Disorder with IUPred2A (2020, methodology): “In this new implementation, we reparametrized ANCHOR on newly available datasets, such as the comprehensive database of disordered proteins DisProt (Piovesan et al., 2017) and complexes of ordered and disordered proteins (Schad et al., 2018).”