Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.

Szczegóły
Abstrakt

Tytuł:: Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.
Autorzy:: Bhattarai A; Bioinformatics Programming Laboratory, Department of Biotechnology, School of Biosciences and Technology, Vellore Institute of Technology, Vellore 632 014, India.
Emerson IA
Źródło:: Journal of biosciences [J Biosci] 2020; Vol. 45.
Typ publikacji:: Journal Article; Review
Język:: English
Imprint Name(s):: Publication: <2006- >: New Delhi : Springer India, in co-publication with Indian Academy of Sciences
Original Publication: [Bangalore] : Indian Academy of Sciences, 1979-
MeSH Terms:: Protein Conformation*
Protein Stability*
Intrinsically Disordered Proteins/*chemistry
Intrinsically Disordered Proteins/*metabolism
Drug Delivery Systems ; Protein Binding ; Protein Domains ; Protein Folding
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Substance Nomenclature:: 0 (Intrinsically Disordered Proteins)
Entry Date(s):: Date Created: 20200206 Date Completed: 20201008 Latest Revision: 20210217
Update Code:: 20240105
PMID:: 32020911
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Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition upon binding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatory processes. This review mainly focuses on the dynamics of disordered proteins including their conformational heterogeneity, protein-protein interactions, and the phase transition of biomolecular condensates that are central to various biological functions. Besides, the role of RNA-mediated chaperones in protein folding and stability of IDPs were also discussed. Finally, we explored the dynamic binding interface of IDPs as novel therapeutic targets and the effect of small molecules on their interactions.

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