Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask, Canada.
Biochem Biophys Res Commun. 2010 Jan 1;391(1):224-9. doi: 10.1016/j.bbrc.2009.11.036. Epub 2009 Nov 10.
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.
中枢神经系统髓鞘是一种动态实体，起源于从少突胶质细胞延伸出来的膜过程，少突胶质细胞在神经元周围形成紧密包裹的多层结构。在成熟的髓鞘中，经典 MBP 的主要剪接异构体为 18.5kDa。在溶液中，MBP 是一种伸展的、固有无序的蛋白质，具有用于多种相互作用的大有效蛋白质表面，并具有用于分子缔合或识别的瞬时和/或诱导的有序二级结构元件。在这里，我们通过纳米孔分析表明，二价阳离子铜和锌在体外诱导伸展蛋白的紧缩，提示可能反映其在髓鞘中排列的三级构象。
