Article
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Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins
Version 1
: Received: 24 April 2024 / Approved: 24 April 2024 / Online: 24 April 2024 (15:35:56 CEST)
How to cite: Venati, S. R.; Uversky, V. N. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins. Preprints 2024, 2024041628. https://doi.org/10.20944/preprints202404.1628.v1 Venati, S. R.; Uversky, V. N. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins. Preprints 2024, 2024041628. https://doi.org/10.20944/preprints202404.1628.v1
Abstract
In this work, we explore the intrinsic disorder status of the three members of the synuclein family of proteins - α-, β-, and γ-synucleins. We also analyzed the peculiarities of the amino acid sequences and modeled 3D structures of the human synuclein family members to find potential effects of pathological mutations. Furthermore, we conducted a comparative sequence-based analysis of the synuclein proteins from various evolutionary distant species and evaluated their levels of intrinsic disorder using a set of commonly used bioinformatics tools. Next, we conducted a detailed functional disorder analysis of the proteins in the interactomes of the human synuclein family members using various web-based disorder analysis and prediction tools, such as RIDAO, D2P2 and FuzDrop. We identify that the interactome of human α-synuclein has relatively higher levels of intrinsic disorder, as compared to the interactomes of human β- and γ- synucleins. These observations highlight the critical importance of intrinsic disorder of human α-synuclein and its interactors in neuronal processes as compared to other proteins of the synuclein family.
Keywords
α-synuclein; β-synuclein; γ-synuclein; intrinsically disordered protein; liquid-liquid phase separation; Parkinson’s disease; protein-protein interactions
Subject
Biology and Life Sciences, Life Sciences
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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