From multifunctionality to polypathogenicity with intrinsic disorder
Konferencijski prilog (Objavljena verzija)
,
© 2023 Institute of Molecular Genetics and Genetic Engineering, University of Belgrade
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structure
under physiological conditions in vitro. IDPs are characterized by an astonishing multilevel
spatiotemporal heterogeneity, with their mosaic structure representing a complex
combination of foldons, inducible foldons, morphing inducible foldons, non-foldons, semifoldons,
and unfoldons.
IDPs are highly abundant in nature and have functional repertoire that is very
broad and complements functions of ordered proteins. Often, IDPs are involved in
regulation, signaling and control pathways, commonly acting as hubs in protein-protein
interaction networks. Intrinsic disorder is an important constituent of the proteoform
concept, representing one of the important means of functional diversification of the
proteinaceous products of a gene. Functions of IDPs may arise from specific disordered
forms, from inter-conversion of disordered forms, or from order ←→ disorder transitions.
The choice betwee...n these conformations is determined by the peculiarities of the
protein environment, and many IDPs possess an exceptional ability to differently fold in a
template-dependent manner. As a result, many IDPs are capable of conducting multiple
functions, with such multifunctionality being linked to their spatiotemporal heterogeneity.
Therefore, a correlation between protein structure and function represents a “protein
structure–function continuum”, where a given protein exists as a dynamic conformational
ensemble containing multiple proteoforms characterized by diverse structural features
and miscellaneous functions.
IDPs are tightly controlled in the norm by various genetic and non-genetic mechanisms.
Alteration in regulation of this disordered regulators are often detrimental to a cell, and
many IDPs are associated with a variety of human diseases, such as cancer, cardiovascular
disease, amyloidoses, neurodegenerative diseases, diabetes and others. Furthermore,
many IDPs are multipathogenic, being associated with the origination and development
of a number of different diseases. Therefore, there is a though-provoking interconnection
between intrinsic disorder, cell signaling, and human diseases, with polypathogenicity of
the involved proteins being linked to their structural plasticity and multifunctionality.
Ključne reči:
intrinsically disordered protein / multifunctionality / polypathogenicity / structurefunction continuumIzvor:
4th Belgrade Bioinformatics Conference, 2023, 4, 23-23Izdavač:
- Belgrade : Institute of molecular genetics and genetic engineering
Napomena:
- Book of abstract: 4th Belgrade Bioinformatics Conference, June 19-23, 2023
Kolekcije
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - CONF AU - N. Uversky, Vladimir PY - 2023 UR - https://belbi.bg.ac.rs/ UR - https://imagine.imgge.bg.ac.rs/handle/123456789/1958 AB - Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structure under physiological conditions in vitro. IDPs are characterized by an astonishing multilevel spatiotemporal heterogeneity, with their mosaic structure representing a complex combination of foldons, inducible foldons, morphing inducible foldons, non-foldons, semifoldons, and unfoldons. IDPs are highly abundant in nature and have functional repertoire that is very broad and complements functions of ordered proteins. Often, IDPs are involved in regulation, signaling and control pathways, commonly acting as hubs in protein-protein interaction networks. Intrinsic disorder is an important constituent of the proteoform concept, representing one of the important means of functional diversification of the proteinaceous products of a gene. Functions of IDPs may arise from specific disordered forms, from inter-conversion of disordered forms, or from order ←→ disorder transitions. The choice between these conformations is determined by the peculiarities of the protein environment, and many IDPs possess an exceptional ability to differently fold in a template-dependent manner. As a result, many IDPs are capable of conducting multiple functions, with such multifunctionality being linked to their spatiotemporal heterogeneity. Therefore, a correlation between protein structure and function represents a “protein structure–function continuum”, where a given protein exists as a dynamic conformational ensemble containing multiple proteoforms characterized by diverse structural features and miscellaneous functions. IDPs are tightly controlled in the norm by various genetic and non-genetic mechanisms. Alteration in regulation of this disordered regulators are often detrimental to a cell, and many IDPs are associated with a variety of human diseases, such as cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, diabetes and others. Furthermore, many IDPs are multipathogenic, being associated with the origination and development of a number of different diseases. Therefore, there is a though-provoking interconnection between intrinsic disorder, cell signaling, and human diseases, with polypathogenicity of the involved proteins being linked to their structural plasticity and multifunctionality. PB - Belgrade : Institute of molecular genetics and genetic engineering C3 - 4th Belgrade Bioinformatics Conference T1 - From multifunctionality to polypathogenicity with intrinsic disorder EP - 23 SP - 23 VL - 4 UR - https://hdl.handle.net/21.15107/rcub_imagine_1958 ER -
@conference{ author = "N. Uversky, Vladimir", year = "2023", abstract = "Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structure under physiological conditions in vitro. IDPs are characterized by an astonishing multilevel spatiotemporal heterogeneity, with their mosaic structure representing a complex combination of foldons, inducible foldons, morphing inducible foldons, non-foldons, semifoldons, and unfoldons. IDPs are highly abundant in nature and have functional repertoire that is very broad and complements functions of ordered proteins. Often, IDPs are involved in regulation, signaling and control pathways, commonly acting as hubs in protein-protein interaction networks. Intrinsic disorder is an important constituent of the proteoform concept, representing one of the important means of functional diversification of the proteinaceous products of a gene. Functions of IDPs may arise from specific disordered forms, from inter-conversion of disordered forms, or from order ←→ disorder transitions. The choice between these conformations is determined by the peculiarities of the protein environment, and many IDPs possess an exceptional ability to differently fold in a template-dependent manner. As a result, many IDPs are capable of conducting multiple functions, with such multifunctionality being linked to their spatiotemporal heterogeneity. Therefore, a correlation between protein structure and function represents a “protein structure–function continuum”, where a given protein exists as a dynamic conformational ensemble containing multiple proteoforms characterized by diverse structural features and miscellaneous functions. IDPs are tightly controlled in the norm by various genetic and non-genetic mechanisms. Alteration in regulation of this disordered regulators are often detrimental to a cell, and many IDPs are associated with a variety of human diseases, such as cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, diabetes and others. Furthermore, many IDPs are multipathogenic, being associated with the origination and development of a number of different diseases. Therefore, there is a though-provoking interconnection between intrinsic disorder, cell signaling, and human diseases, with polypathogenicity of the involved proteins being linked to their structural plasticity and multifunctionality.", publisher = "Belgrade : Institute of molecular genetics and genetic engineering", journal = "4th Belgrade Bioinformatics Conference", title = "From multifunctionality to polypathogenicity with intrinsic disorder", pages = "23-23", volume = "4", url = "https://hdl.handle.net/21.15107/rcub_imagine_1958" }
N. Uversky, V.. (2023). From multifunctionality to polypathogenicity with intrinsic disorder. in 4th Belgrade Bioinformatics Conference Belgrade : Institute of molecular genetics and genetic engineering., 4, 23-23. https://hdl.handle.net/21.15107/rcub_imagine_1958
N. Uversky V. From multifunctionality to polypathogenicity with intrinsic disorder. in 4th Belgrade Bioinformatics Conference. 2023;4:23-23. https://hdl.handle.net/21.15107/rcub_imagine_1958 .
N. Uversky, Vladimir, "From multifunctionality to polypathogenicity with intrinsic disorder" in 4th Belgrade Bioinformatics Conference, 4 (2023):23-23, https://hdl.handle.net/21.15107/rcub_imagine_1958 .