Pritišanac Lab
Approximately 60% of human proteins contain long segments lacking stable secondary or tertiary structures, known as intrinsically disordered protein regions (IDRs). These regions are increasingly recognized as key regulators of a wide range of cellular processes, including mRNA transcription, splicing, protein translation, signal transduction, and localization in specific biomolecular condensates. Furthermore, IDRs are enriched in risk genes associated with complex diseases, including neurodevelopmental disorders and cancer (Tsang, Pritišanac et al. 2020 Cell). To perform their functions, IDRs engage in intra- and intermolecular interactions that are typically transient and highly dynamic, and they can adapt their interfaces depending on their binding partner (Alderson & Pritišanac, et al. 2023 PNAS).
IDRs are also highly enriched in risk genes associated with complex diseases, including neurodevelopmental disorders and cancer (Tsang, Pritišanac et al. 2020 Cell). Our research aims to deepen our understanding of molecular recognition in the dynamic regions of the proteome and transcriptome. By combining computational structural biology, cutting-edge AI models, bioinformatics, and protein NMR spectroscopy, we seek to understand, predict, and design tunable biomolecular interactions that are crucial for health and disease pathology. Together with our partners, we conduct research ranging from basic research and drug discovery to the interpretation of disease variants and protein engineering.
Network: In addition to collaborations within the Otto Loewi Research Center and the Medical University of Graz, we work with researchers from around the world. Our cooperation partners include Reid Alderson (Helmholtz Munich), Lu-Yang Wang (SickKids Toronto), Jason Moffat (University of Toronto), Anne Conibear (TU Wien), Vaclav Veverka (Charles University) and Matteo Degiacomi (Durham University).
Approximately 60% of human proteins contain long segments lacking stable secondary or tertiary structures, known as intrinsically disordered protein regions (IDRs). These regions are increasingly recognized as key regulators of a wide range of cellular processes, including mRNA transcription, splicing, protein translation, signal transduction, and localization in specific biomolecular condensates. Furthermore, IDRs are enriched in risk genes associated with complex diseases, including neurodevelopmental disorders and cancer (Tsang, Pritišanac et al. 2020 Cell). To perform their functions, IDRs engage in intra- and intermolecular interactions that are typically transient and highly dynamic, and they can adapt their interfaces depending on their binding partner (Alderson & Pritišanac, et al. 2023 PNAS).
IDRs are also highly enriched in risk genes associated with complex diseases, including neurodevelopmental disorders and cancer (Tsang, Pritišanac et al. 2020 Cell). Our research aims to deepen our understanding of molecular recognition in the dynamic regions of the proteome and transcriptome. By combining computational structural biology, cutting-edge AI models, bioinformatics, and protein NMR spectroscopy, we seek to understand, predict, and design tunable biomolecular interactions that are crucial for health and disease pathology. Together with our partners, we conduct research ranging from basic research and drug discovery to the interpretation of disease variants and protein engineering.
Network: In addition to collaborations within the Otto Loewi Research Center and the Medical University of Graz, we work with researchers from around the world. Our cooperation partners include Reid Alderson (Helmholtz Munich), Lu-Yang Wang (SickKids Toronto), Jason Moffat (University of Toronto), Anne Conibear (TU Wien), Vaclav Veverka (Charles University) and Matteo Degiacomi (Durham University).
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