MFIB Edit

Citations: 6

z-index: 3

Basic information
Short name MFIB
Full name mutual folding induced by binding
Description 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.
URL http://mfib.enzim.ttk.mta.hu
Year founded 2017
Last update & version 26-06-2017
Accessibility Accessible
Contact information

The contact information is provided to facilitate update of database information, and it is curated based on the contact details in the database or the related publications. To ensure effective contact with database constructors, we give priority to the contact details in the database.

University/Institution Institute of Enzymology, Hungarian Academy of Sciences
Address Institute of Enzymology, RCNS, Hungarian Academy of Sciences, 'Momentum' Membrane Protein Bioinformatics Research Group, Budapest H-1117, Hungary
City
Province/State
Country/Region Hungary
Contact name (PI/Team) Mészáros B
Contact email (PI/Helpdesk) meszaros.balint@ttk.mta.hu
Data information
Data object
Data type
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Keyword
Publications
  • MFIB: a repository of protein complexes with mutual folding induced by binding. [PMID: 29036655]
    Erzsébet Fichó, István Reményi, István Simon, Bálint Mészáros,

    Motivation: It is commonplace that intrinsically disordered proteins (IDPs) are involved in crucial interactions in the living cell. However, the study of protein complexes formed exclusively by IDPs is hindered by the lack of data and such analyses remain sporadic. Systematic studies benefited other types of protein-protein interactions paving a way from basic science to therapeutics; yet these efforts require reliable datasets that are currently lacking for synergistically folding complexes of IDPs.
    Results: Here we present the Mutual Folding Induced by Binding (MFIB) database, the first systematic collection of complexes formed exclusively by IDPs. MFIB contains an order of magnitude more data than any dataset used in corresponding studies and offers a wide coverage of known IDP complexes in terms of flexibility, oligomeric composition and protein function from all domains of life. The included complexes are grouped using a hierarchical classification and are complemented with structural and functional annotations. MFIB is backed by a firm development team and infrastructure, and together with possible future community collaboration it will provide the cornerstone for structural and functional studies of IDP complexes.
    Availability and implementation: MFIB is freely accessible at http://mfib.enzim.ttk.mta.hu/. The MFIB 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: simon.istvan@ttk.mta.hu, meszaros.balint@ttk.mta.hu.
    Supplementary information: Supplementary data are available at Bioinformatics online.

    Bioinformatics 2017:33(22)

    6 Citations (from Europe PMC, 2019-06-22)

Rank

  • Ranking in all databases: No. 1823
  • Ranking in category/categories:
    • Structure: No. 238
    • Interaction: No. 278
The box plots depict Z-index distribution for all databases in Database Commons and for specific database category/categories. The red line indicates log2(Z-index) of MFIB.

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Cited

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Record metadata

  • Created on: 2018-01-28
    • ***ina@***c.cn [2019-06-10]
    • ***ashireen@***u.edu.pk [2018-04-09]
    • ***ngyang17m@***c.cn [2018-01-28]

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