title: Understanding pre-structured motifs (PreSMos) in intrinsically unfolded proteins.
abstract: 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.
authors: Biomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, 125 Gwahak-ro, Yuseong-gu, Daejeon, 305-806 Korea.
authors: Si-Hyung
authors: SH
authors: Lee
authors: Do-Hyoung
authors: DH
authors: Kim
authors: Joan J
authors: JJ
authors: Han
authors: Eun-Ji
authors: EJ
authors: Cha
authors: Ji-Eun
authors: JE
authors: Lim
authors: Ye-Jin
authors: YJ
authors: Cho
authors: Chewook
authors: C
authors: Lee
authors: Kyou-Hoon
authors: KH
authors: Han
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins