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The lipid specificities of two related integral membrane proteins of central nervous system myelin, the proteolipid (PLP) and DM-20 proteins, which differ only by the deletion of a polar stretch of 35 contiguous amino acid residues, were studied with spin-labeled lipids after reconstitution into dimyristoyl-phosphatidylcholine. The selectivity in populating lipid association sites at the protein interface and in modulating the lipid exchange between protein and bulk lipid sites was quantitated by the relative association constants and the off-rate constants for exchange, respectively, for both proteins. The sequence deleted in DM-20 (residues 116-150 of PLP) is found to play a major role in determining the lipid selectivity for the parent PLP protein.

biochemistry

Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin-label ESR studies with DM-20/lipid recombinants