IDPpi: Protein-Protein Interaction Analyses of Human Intrinsically Disordered Proteins

Scientific Reports
Vladimir PerovicNevena Veljkovic

Abstract

Intrinsically disordered proteins (IDPs) are characterized by the lack of a fixed tertiary structure and are involved in the regulation of key biological processes via binding to multiple protein partners. IDPs are malleable, adapting to structurally different partners, and this flexibility stems from features encoded in the primary structure. The assumption that universal sequence information will facilitate coverage of the sparse zones of the human interactome motivated us to explore the possibility of predicting protein-protein interactions (PPIs) that involve IDPs based on sequence characteristics. We developed a method that relies on features of the interacting and non-interacting protein pairs and utilizes machine learning to classify and predict IDP PPIs. Consideration of both sequence determinants specific for conformational organizations and the multiplicity of IDP interactions in the training phase ensured a reliable approach that is superior to current state-of-the-art methods. By applying a strict evaluation procedure, we confirm that our method predicts interactions of the IDP of interest even on the proteome-scale. This service is provided as a web tool to expedite the discovery of new interactions and IDP functio...Continue Reading

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Citations

Jul 7, 2019·Amino Acids·Neven SumonjaVladimir Perovic
May 7, 2019·Frontiers in Oncology·Markus Hartl, Rainer Schneider
Dec 8, 2020·The FEBS Journal·Gesa RichterTobias Madl
Jun 9, 2021·The Biochemical Journal·Kaare TeilumBirthe B Kragelund
Jul 18, 2021·Protein Science : a Publication of the Protein Society·Sarah F RuidiazBirthe B Kragelund
Apr 2, 2021·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Emmanuel PrikasArne Ittner

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Methods Mentioned

BETA
immunoprecipitation
protein folding

Software Mentioned

HIPPIE
ReviGO
CD
Hit
BiNGO
Cytoscape
NextProt
NCBO Annotator service
PAAC
NCBO Annotator

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