Divalent cations induce a compaction of intrinsically disordered myelin basic protein.
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 18.5kDa. 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.
Baran
Christian
C
Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask, Canada.
Smith
Graham S T
GS
Bamm
Vladimir V
VV
Harauz
George
G
Lee
Jeremy S
JS
D000818:Animals; D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry*; D051379:Mice; D004676:Myelin Basic Protein; D049329:Nanostructures; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D016062:Porosity; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D015032:Zinc / Q000737:chemistry*
D002413:Cations, Divalent; C499047:Mbp protein, mouse; D004676:Myelin Basic Protein; D009419:Nerve Tissue Proteins; D011994:Recombinant Proteins; D014157:Transcription Factors; D003300:Copper; D015032:Zinc