Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 13, Issue 1, Pages 34-54Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920312799277974
Keywords
PreSMos (Pre-Structured Motifs); IUPs (Intrinsically Unfolded Proteins); NMR; IDR (Intrinsically Disordered Region); Mostly Unstructured (MU); Completely Unstructured (CU)
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Funding
- Korea Research Council of Fundamental Science and Technology (KRCF)
- Korea Research Foundation (KRF) [2010-0022224]
- National Research Foundation of Korea [2010-0022224] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Intrinsically unfolded proteins (IUPs) do not obey the golden rule of structural biology, 3D structure = function, as they manifest their inherent functions without resorting to three-dimensional structures. Absence of a compact globular topology in these proteins strongly implies that their ligand recognition processes should involve factors other than spatially well-defined binding pockets. Heteronuclear multidimensional (HetMulD) NMR spectroscopy assisted with a stable isotope labeling technology is a powerful tool for quantitatively investigating detailed structural features in IUPs. In particular, it allows us to delineate the presence and locations of pre-structured motifs (PreSMos) on a per-residue basis. PreSMos are the transient local structural elements that presage target-bound conformations and act as specificity determinants for IUP recognition by target proteins. Here, we present a brief chronicle of HetMulD NMR studies on IUPs carried out over the past two decades along with a discussion on the functional significance of PreSMos in IUPs.
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