FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies
By Márton Miskei, Csaba Antal, Mónika Fuxreiter. 2016
106 citations recorded by the source corpus.
FuzDB (http://protdyn-database.org) compiles experimentally observed fuzzy protein complexes, where intrinsic disorder (ID) is maintained upon interacting with a partner (protein, nucleic acid or small molecule) and directly impacts biological function. Entries in the database have both (i) structural evidence demonstrating the structural multiplicity or dynamic disorder of the ID region(s) in the partner bound form of the protein and (ii) in vitro or in vivo biological evidence that indicates the significance of the fuzzy region(s) in the formation, function or regulation of the assembly. Unlike the other intrinsically disordered or unfolded protein databases, FuzDB focuses on ID regions within a biological context, including higher-order assemblies and presents a detailed analysis of the structural and functional data. FuzDB also provides interpretation of experimental results to elucidate the molecular mechanisms by which fuzzy regions—classified on the basis of topology and mechanism—interfere with the structural ensembles and activity of protein assemblies. Regulatory sites generated by alternative splicing (AS) or post-translational modifications (PTMs) are also collected. By assembling all this information, FuzDB could be utilized to develop stochastic structure–function relationships for proteins and could contribute to the emergence of a new paradigm.
Subfields: Molecular Biology
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In Molecular Biology
- Zsuzsanna Dosztányi
- Gábor Erdös
- Bálint Mészáros
- Vladimir N Uversky
- Michele Vendruscolo
- Damiano Piovesan
- Silvio C. E. Tosatto
- Lukasz Kurgan
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “While the majority of known disordered binding regions lose their flexibility upon interaction (with the exception of fuzzy complexes (6,7)), an order-to-disorder transition is the key for the function of another group of proteins.”
- MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017, background): “FuzDB collects cases of fuzzy complexes, where conformational diversity has a functional role in the regulation and formation of protein complexes or higher-order assemblies.”
- Analyzing Protein Disorder with IUPred2A (2020, background): “However, some IDRs retain a significant amount of flexibility even in the bound form, forming fuzzy complexes (Borgia et al., 2018; Miskei, Antal, & Fuxreiter, 2017).”