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.
Keywords: PreSMos (Pre-Structured Motifs), IUPs (Intrinsically Unfolded Proteins), NMR, IDR (Intrinsically Disordered Region), Mostly Unstructured (MU), Completely Unstructured (CU), IDPs, NUPs, Polypeptide, amphipathic helix
Current Protein & Peptide Science
Title: Understanding Pre-Structured Motifs (PreSMos) in Intrinsically Unfolded Proteins
Volume: 13 Issue: 1
Author(s): Si-Hyung Lee, Do-Hyoung Kim, Joan J. Han, Eun-Ji Cha, Ji-Eun Lim, Ye-Jin Cho, Chewook Lee and Kyou-Hoon Han
Affiliation:
Keywords: PreSMos (Pre-Structured Motifs), IUPs (Intrinsically Unfolded Proteins), NMR, IDR (Intrinsically Disordered Region), Mostly Unstructured (MU), Completely Unstructured (CU), IDPs, NUPs, Polypeptide, amphipathic helix
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.
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Cite this article as:
Lee Si-Hyung, Kim Do-Hyoung, J. Han Joan, Cha Eun-Ji, Lim Ji-Eun, Cho Ye-Jin, Lee Chewook and Han Kyou-Hoon, Understanding Pre-Structured Motifs (PreSMos) in Intrinsically Unfolded Proteins, Current Protein & Peptide Science 2012; 13 (1) . https://dx.doi.org/10.2174/138920312799277974
DOI https://dx.doi.org/10.2174/138920312799277974 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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