Mol. Cells 2018; 41(10):   https://doi.org/10.14348/molcells.2018.0192
PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins
Do-Hyoung Kim, and Kyou-Hoon Han*
Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Korea
*Correspondence: khhan600@kribb.re.kr
Received May 2, 2018; Revised August 7, 2018; Accepted August 22, 2018.; Published online September 30, 2018.
© Korean Society for Molecular and Cellular Biology. All rights reserved.

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit (http://creativecommons.org/licenses/by-nc-sa/3.0/).
ABSTRACT
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.
Keywords: IDPs, IDR (Intrinsically Disordered Region), NMR, IUPs (Intrinsically Unfolded Proteins), PreSMos (Pre-Structured Motifs)


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30 September 2018 Volume 41,
Number 9, pp. 809~880

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