IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding

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ID: 294496
2018
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Abstract
The structural states of proteins include ordered globular domains as well as intrinsically disordered protein regions that exist as highly flexible conformational ensembles in isolation.Various computational tools have been developed to discriminate ordered and disordered segments based on the amino acid sequence.However, properties of IDRs can also depend on various conditions, including binding to globular protein partners or environmental factors, such as redox potential.These cases provide further challenges for the computational characterization of disordered segments.In this work we present IUPred2A, a combined web interface that allows to generate energy estimation based predictions for ordered and disordered residues by IUPred2 and for disordered binding regions by ANCHOR2.The updated web server retains the robustness of the original programs but offers several new features.While only minor bug fixes are implemented for IUPred, the next version of ANCHOR is significantly improved through a new architecture and parameters optimized on novel datasets.In addition, redox-sensitive regions can also be highlighted through a novel experimental feature.The web server offers graphical and text outputs, a RESTful interface, access to software download and extensive help, and can be accessed at a new location: http://iupred2a.elte.hu.
Reference Key
openalex_W2806884808 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Bálint Mészáros, Gábor Erdős, Zsuzsanna Dosztányi
Journal Nucleic Acids Research
Year 2018
DOI
10.1093/nar/gky384
URL
https://doi.org/10.1093/nar/gky384
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