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Open questions: Reflections on intrinsically disordered proteins [PDF]
Network Biology, 2021 Intrinsically Disordered Proteins or Regions (IDPs) are proteins that lack a predetermined 3D structure playing key cellular functions including regulation, signaling, and protein-protein/DNA interaction.
Mouna Choura, Ahmed Rebai
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BMC Bioinformatics, 2017 Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu +8 more
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
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Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family [PDF]
, 2013 Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng +19 more
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Intrinsically disordered proteins: modes of binding with emphasis on disordered domains
Open Biology, 2021 Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris +2 more
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Intrinsic disorder in putative protein sequences [PDF]
Proteome Science, 2011 Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradovic
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Intrinsically Disordered Proteins in Chronic Diseases
Biomolecules, 2019 It is now increasingly evident that a large fraction of the human proteome comprises proteins that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have segments that are not likely to form a defined 3D structure [...]
Prakash Kulkarni, Vladimir N. Uversky
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Self‐recognition by an intrinsically disordered protein [PDF]
FEBS Letters, 2008 The intrinsically disordered translocation domain (T‐domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T‐domain of colicin N known to bind to the helper protein TolA in target cells also ...
Hecht O +7 more
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Targeting Intrinsically Disordered Proteins through Dynamic Interactions
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) are over-represented in major disease pathways and have attracted significant interest in understanding if and how they may be targeted using small molecules for therapeutic purposes.
Jianlin Chen, Xiaorong Liu, Jianhan Chen
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Ensemble Docking for Intrinsically Disordered Proteins. [PDF]
J Chem Inf ModelAbstract Intrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable for IDPs.
Dhar A, Sisk TR, Robustelli P.
europepmc +4 more sources