期刊
MICRON
卷 35, 期 7, 页码 503-542出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micron.2004.04.005
关键词
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
类别
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 (similar to75%) of random coil, but postulated to have core elements of beta-sheet and alpha-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. (C) 2004 Elsevier Ltd. All rights reserved.
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