DIBS is developed and maintained by the Bioinformatics Research Group of the Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences.

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Citing DIBS:

Eva Schad, Erzsébet Fichó, Rita Pancsa, István Simon, Zsuzsanna Dosztányi and Bálint Mészáros:
DIBS: a repository of disordered binding sites mediating interactions with ordered proteins
Bioinformatics. 2018 February 1; 34(3):535-537
PMID: 29385418
doi: 10.1093/bioinformatics/btx640

News 20.10.2017

Our paper was published in Bioinformatics:
doi: 10.1093/bioinformatics/btx640

News 08.10.2017

Our manuscript was accepted in Bioinformatics.

News 28.09.2017

DIBS has been updated and expanded. The database now includes 1,577 structures grouped into 773 entries. The biological annotations based on GO were refined and revised for all entries to significantly expand the level of annotation.

News 28.07.2017

The Disordered Binding Site (DIBS) database is launched. The current version of the database is 28-07-2017 and contains 714 entries.

The DIBS server is a platform to offer access to the database. If you have any comments or find a problem to report, contact us at: dibs(at)ttk.mta.hu

Disordered Binding Site (DIBS) database is a repository for protein complexes that are formed between Intrinsically Disordered Proteins (IDPs) and globular/ordered partner proteins. While ordered proteins have a well-defined tertiary structure on their own, IDPs are highly flexible fluctuating between a large number of alternative conformations.

IDPs in general perform functions vital to living organisms. They are typically deeply embedded in signaling and regulatory pathways, play pivotal roles in transcription, stress-response, host-pathogen interactions and the development of a wide range of pathological states. Most functions of IDPs that enable their involvement in these processes depend on their interactions with other protein partners. Upon interaction with ordered proteins, IDPs generally adopt a stable structure in a process termed coupled-folding-and-binding. In these cases the pre-existing surface of the ordered partner serves as a structural platform for the emerging structure of the IDP.

Since the systematic study of IDPs have been undertaken, a wealth of information has been accumulated about their biological functions, mechanisms of action and their abundance in (especially higher order) organisms. These information are integrated into a large number of fundamental databases, such as UniProt and are also collected in IDP-specific databases, such as DisProt, IDEAL or MobiDB. Interacting regions of IDPs are collected in specific databases, such as DisBind. A more specialized database, FuzDB provides a wealth of examples about cases where IDPs do not fully undergo a disorder-to-order transition upon binding. Furthermore, as interacting sites of IDPs often recognize their partners via linear motifs, motif databases, such as ELM contain several bound IDP structures. In addition, binding sites in IDPs that bind to ordered proteins can be predicted from the protein sequence alone using various bioinformatics tools, such as ANCHOR or MoRFchibi System.

DIBS presents by far the largest collection of IDPs capable of binding to and folding upon the surface of ordered protein partners. Apart from functional information and atomic-level structural annotations, DIBS also incorporates information on binding strength by providing Kd values for the majority of interactions, and also includes entries with functionally relevant post-translational modifications on the IDP chain (often substantially modulating the binding strength) where such complex structures are available. Together with its sister database, MFIB (that describes protein complexes formed exclusively by disordered proteins), DIBS covers the known spectrum of protein-protein interactions mediated by IDPs.