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. 2018 Feb 1;34(3):535-537.
doi: 10.1093/bioinformatics/btx640.

DIBS: a repository of disordered binding sites mediating interactions with ordered proteins

Eva Schad  1 , Erzsébet Fichó  1 , Rita Pancsa  2 , István Simon  1 , Zsuzsanna Dosztányi  3 , Bálint Mészáros  1   3
Affiliations

DIBS: a repository of disordered binding sites mediating interactions with ordered proteins

Eva Schad et al. Bioinformatics. .

Abstract

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.

Contact: dosztanyi@caesar.elte.hu or bmeszaros@caesar.elte.hu.

Supplementary information: Supplementary data are available at Bioinformatics online.

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Figures

Fig. 1
Fig. 1
Kd values in DIBS. Distribution of Kd values of interactions in DIBS (top), together with three selected examples with differing biological functions and, correspondingly, differing Kds (bottom). Interactions 2 and 3 contain the same disordered protein segment in different post-translational modification states binding to different partners
Fig. 2
Fig. 2
Distribution of data in DIBS. (A) Distribution of DIBS entries with regards to various types of disorder annotation. Dark grey boxes represent entries for which Kd values are available and light grey boxes mark entries without known Kd values. (B) Taxonomic distribution of the 773 complexes in DIBS (B—Bacteria, V—Viruses, C—Cross-domain interactions). While archaeal proteins form parts of cross-domain interactions, no purely archaeal interactions are currently available
See this image and copyright information in PMC

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