PreSMo target-binding signatures in intrinsically disordered proteins

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PreSMo target-binding signatures in intrinsically disordered proteins
Do-hyoung Kim; Kyou Hoon Han
Bibliographic Citation
Molecules and Cells, vol. 41, no. 10, pp. 889-899
Publication Year
Intrinsically disordered proteins (IDPs) are highly unorthodox proteins that do not form three-dimensional structures under physiological conditions. The discovery of IDPs has destroyed the classical structure-function paradigm in protein science, 3-D structure = function, because IDPs even without well-folded 3-D structures are still capable of performing important biological functions and furthermore are associated with fatal diseases such as cancers, neurodegenerative diseases and viral pandemics. Pre-structured motifs (PreSMos) refer to transient local secondary structural elements present in the target-unbound state of IDPs. During the last two decades PreSMos have been steadily acknowledged as the critical determinants for target binding in dozens of IDPs. To date, the PreSMo concept provides the most convincing structural rationale explaining the IDP-target binding behavior at an atomic resolution. Here we present a brief developmental history of PreSMos and describe their common characteristics. We also provide a list of newly discovered PreSMos along with their functional relevance.
IUPs (Intrinsically Unfolded Proteins)NMRPreSMos (Pre-Structured Motifs)IDR (Intrinsically Disordered Region)IDPs
Korea Soc-Assoc-Inst
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Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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