Publication | Open Access
The structure of bovine brain myelin proteolipid and its organization in myelin.
137
Citations
20
References
1984
Year
Proteinlipid InteractionMyelin ProteolipidBovine Brain MyelinCytoskeletonLipid MovementCellular NeurobiologyCellular PhysiologySocial SciencesProtein FoldingMembrane TransportExperimental NeuropathologyBiophysicsAnimal PhysiologyMolecular NeuroscienceBiochemistryMyelin MembraneNervous SystemCell BiologyMultilamellar Myelin StructureNeurophysiologyNeuroanatomyPhysiologyNeuroscienceCentral Nervous SystemIntracellular TraffickingMedicine
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.
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