MFIB 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 MFIB:

Erzsébet Fichó, István Reményi, István Simon and Bálint Mészáros:
MFIB: a repository of protein complexes with mutual folding induced by binding
Bioinformatics. 2017 Nov 15; 33(22):3682-3684
PMID: 29036655
doi: 10.1093/bioinformatics/btx486

Access the recommendation on F1000Prime

News 08.06.2018

The embedded structure viewer has been updated to LiteMol to enhance speed and usability.

News 18.11.2017

Another F1000Prime recommendation by F1000 Faculty Member Alexandre Bonvin.

News 14.11.2017

Our paper has been recommended in F1000Prime as being of special significance in its field by F1000 Faculty Member Vladimir Uversky.

News 13.09.2017

Our paper was published in Bioinformatics:
doi: 10.1093/bioinformatics/btx486

News 26.07.2017

Our manuscript was accepted in Bioinformatics.

News 26.06.2017

The current version of the database is 26-06-2017, containing 1,406 structures grouped into 205 entries. All databases used for the construction of MFIB were updated: PDB (28-03-2017), DisProt (version 7 v0.4), Pfam (version 31.0) and IDEAL (version 29-03-2017). The "Help" and "Statistics" pages were also updated.

News 24.02.2017

Mutual Folding Induced by Binding (MFIB) database is launched. The current version of the database is 23-02-2017 and contains 158 entries.

The MFIB server is a platform to offer access to the database. This is currently the public test version of the site. If you have any comments or find a problem to report, contact us at: mfib(at)

Mutual Folding Induced by Binding (MFIB) database is a repository for protein complexes that are formed exclusively by intrinsically unstructured proteins (IUPs). As these proteins have no stable tertiary structure in their monomeric form, their folding is induced by the assembly of the complex.

IUPs 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.

Since the systematic study of IUPs has been undertaken, a wealth of information has been accumulated about their biological functions, mechanisms of action and their abundance in (especially higher order) living organisms. These information are integrated into a large number of fundamental databases, such as UniProt and are also collected in IUP-specific databases, such as DisProt, IDEAL or MobiDB.

Many functions IUPs fulfill depend on their interactions with other protein partners. Upon interaction with ordered proteins, IUPs generally adopt a stable structure in a process termed coupled-folding-and-binding. Such interacting sites of IUPs often recognize their partners via a linear motif and thus linear motif databases, such as ELM contain several bound IUP structures. In addition, binding sites in IUPs that interact with ordered proteins can be predicted from the protein sequence alone using various bioinformatics tools, such as ANCHOR or MoRFchibi System.

MFIB complements the research of IUP interactions by providing a curated and annotated set of complexes that are formed by IUPs alone. In these cases the emerging complex structure does not form on the template surface of an ordered protein. Instead, the folding of all participating protein partners happens at the same time, coupled to the interaction in a synergistic manner. MFIB serves as a collection of such protein complexes together with their structural and functional annotations, as well as links and literature references that describe the experimental verification of the mutual coupled-folding-and-binding process, that is a hallmark of the described complexes.