Structure Determination of an Immunopotentiator Peptide, Cinnamycin, Complexed with Lysophosphatidylethanolamine by 1H-NMR
- 1 February 1996
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 119 (2) , 226-230
- https://doi.org/10.1093/oxfordjournals.jbchem.a021226
Abstract
The three-dimensional structure of a complex of cinnamycin, a 19-amino acid residue immunopotentiator peptide, and lysophosphatidylethanolamine was determined by 1H-NMR. The complex was cylindrical in shape, 11 Å in diameter and 26 Å in length, excluding the acyl chain of the phospholipid. The peptide had a hydrophobic pocket surrounded by . residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanol-amine head group would be unable to fit the pocket. The goodness of the fitting is compatible with the strict specificity of ligand binding of the peptide.Keywords
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