The structure of bovine brain myelin proteolipid and its organization in myelin.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003545:Cysteine; D009185:Myelin Proteins / Q000096:biosynthesis; D018991:Myelin Proteolipid Protein; D009186:Myelin Sheath / Q000648:ultrastructure*; D011487:Protein Conformation; D011510:Proteolipids; D012995:Solubility; D013329:Structure-Activity Relationship; D014867:Water
D009185:Myelin Proteins; D018991:Myelin Proteolipid Protein; D011510:Proteolipids; D014867:Water; D003545:Cysteine