Laursen R A, Samiullah M, Lees M B
Proc Natl Acad Sci U S A. 1984 May;81(9):2912-6. doi: 10.1073/pnas.81.9.2912.
A model, based on amino acid sequence data, is proposed for the organization of the myelin proteolipid in myelin membrane. The model has three distinctive features: three trans-membrane segments that traverse the lipid bilayer, two cis-membrane domains that enter and exit the same side of the membrane, and a highly charged segment resembling myelin basic protein on the cytoplasmic side of the membrane. It is proposed that the cis-membrane domain(s) can promote the formation and stabilization of the multilamellar myelin structure by hydrophobic interaction with the apposite bilayer across the extracellular space.
基于氨基酸序列数据,提出了一种髓磷脂蛋白脂质在髓鞘膜中组织方式的模型。该模型有三个显著特征:三个跨膜片段横穿脂质双层,两个顺膜结构域进出膜的同一侧,以及膜细胞质侧有一个类似髓磷脂碱性蛋白的高电荷片段。有人提出,顺膜结构域可通过与细胞外空间对面的双层进行疏水相互作用,促进多层髓鞘结构的形成和稳定。