MFIB: a repository of protein complexes with mutual folding induced by binding

By Erzsébet Fichó, István Reményi, István Simon, Bálint Mészáros. 2017

70 citations recorded by the source corpus.

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.

Subfields: Cell Biology, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Molecular Biology

Citations in the corpus

IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “Integration with the UniProt resource enables the display of various additional information about the requested protein (when available), such as PFAM annotations (47), low-throughput post-translational modifications (including phosphorylation, methylation and acetylation sites) from PhosphoSitePlus”
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “Overview of databases integrated into MobiDB 3.0 Database Type Comment URL UniProt Curated Disorder http://www.uniprot.org/ DisProt Curated Disorder http://www.disprot.org/ FuzDB Curated Disorder http://protdyn-database.org/ ELM Curated LIPs http://elm.eu.org/ MFIB Curated LIPs http://mfib.enzim.ttk”