期刊
BIOINFORMATICS
卷 34, 期 3, 页码 535-537出版社
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/btx640
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资金
- PostDoc fellowship of the Hungarian Academy of Sciences
- European Molecular Biology Organization [ALTF 702-2015]
- Hungarian Research and Developments Fund [PD-OTKA 108772, OTKA K115698, OTKA K108798]
- Lendulet grant from Hungarian Academy of Sciences [LP2014-18]
- National Research, Development and Innovation Fund of Hungary [FIEK_16-1-2016-0005]
- MRC [MC_U105185859] Funding Source: UKRI
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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