Divalent cations induce a compaction of intrinsically disordered myelin basic protein |
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Authors: | Christian Baran Vladimir V Bamm Jeremy S Lee |
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Institution: | a Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask., Canada S7N 5E5 b Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ont., Canada N1G 2W1 |
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Abstract: | Central nervous system myelin is a dynamic entity arising from membrane processes extended from oligodendrocytes, which form a tightly-wrapped multilamellar structure around neurons. In mature myelin, the predominant splice isoform of classic MBP is 18.5 kDa. In solution, MBP is an extended, intrinsically disordered protein with a large effective protein surface for myriad interactions, and possesses transient and/or induced ordered secondary structure elements for molecular association or recognition. Here, we show by nanopore analysis that the divalent cations copper and zinc induce a compaction of the extended protein in vitro, suggestive of a tertiary conformation that may reflect its arrangement in myelin. |
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Keywords: | Myelin basic protein (MBP) Multiple sclerosis Intrinsically disordered protein Induced folding Nanopore analysis |
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