Understanding pre-structured motifs (PreSMos) in intrinsically unfolded proteins

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Understanding pre-structured motifs (PreSMos) in intrinsically unfolded proteins
Si Hyoung Lee; D H Kim; J J Han; Eun Ji Cha; Ji Eun Lim; Ye Jin Cho; Chewook Lee; Kyou Hoon Han
Bibliographic Citation
Current Protein & Peptide Science, vol. 13, no. 1, pp. 34-54
Publication Year
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.
Completely unstructured (CU)IDR (intrinsically disordered region)IUPs (intrinsically unfolded proteins)Mostly unstructured (MU)NMRPreSMos (pre-structured motifs)
Bentham Science Publ Ltd
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