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  Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz, G., Ishiyama, N., Hill, C. M. D., Bates, I. R., Libich, D. S., & Farès, C. (2004). Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron, 35(7), 503-542. doi:10.1016/j.micron.2004.04.005.

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 Creators:
Harauz, George1, Author
Ishiyama, Noboru1, 2, Author
Hill, Christopher M. D.1, Author
Bates, Ian R.1, 3, Author
Libich, David S.1, Author
Farès, Christophe1, 4, Author           
Affiliations:
1Department of Molecular Biology and Genetics, Biophysics Interdepartmental Group, University of Guelph, Room 230, Axelrod Building, 50 Stone Road East, Guelph, Ont., Canada N1G 2W1, ou_persistent22              
2Department of Biochemistry, McGill University, Montréal, Que., Canada H3A 1A4, ou_persistent22              
3Department of Physiology, McGill University, Montréal, Que., Canada H3G 1Y6, ou_persistent22              
4Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

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Free keywords: 2D crystals; Actin; Calmodulin; Citrulline; Crystallisation; Deimination; Electron crystallography; Electron microscopy; Electron paramagnetic resonance (EPR); Ganglioside; Golli; His-tag; Intrinsically unstructured protein; Magic angle spinning (MAS); MTS-SL (methanethiosulphonate-spin label); Multiple sclerosis; Myelin basic protein; Natively unfolded protein; Nuclear magnetic resonance (NMR); Phosphatidylinositol; Protein–lipid interactions; Recombinant proteins; Site-directed mutagenesis; Site-directed spin labelling (SDSL); Solid-state NMR; Solution NMR
 Abstract: The 18.5 kDa isoform of myelin basic protein (MBP) is a major component of the myelin sheath in the central nervous system of higher vertebrates, and a member of a larger family of proteins with a multiplicity of forms and post-translational modifications (PTMs). The 18.5 kDa protein is the exemplar of the family, being most abundant in adult myelin, and thus the most-studied. It is peripherally membrane-associated, but has generally been investigated in isolated form. MBP is an ‘intrinsically unstructured’ protein with a high proportion (∼75%) of random coil, but postulated to have core elements of β-sheet and α-helix. We review here the properties of the MBP family, especially of the 18.5 kDa isoform, and discuss how its three-dimensional (3D) structure may be resolved by direct techniques available to us, viz., X-ray and electron crystallography, and solution and solid-state NMR spectrometry. In particular, we emphasise that creating an appropriate environment in which the protein can adopt a physiologically relevant fold is crucial to such endeavours. By solving the 3D structure of 18.5 kDa MBP and the effects of PTMs, we will attain a better understanding of myelin architecture, and of the molecular mechanisms that transpire in demyelinating diseases such as multiple sclerosis.

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Language(s): eng - English
 Dates: 2004-07-152004-10-01
 Publication Status: Published in print
 Pages: 40
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.micron.2004.04.005
 Degree: -

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Title: Micron
  Abbreviation : Micron
Source Genre: Journal
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Publ. Info: Oxford/Amsterdam : Pergamon/Elsevier
Pages: - Volume / Issue: 35 (7) Sequence Number: - Start / End Page: 503 - 542 Identifier: ISSN: 0968-4328
CoNE: https://pure.mpg.de/cone/journals/resource/954928585911