Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.
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 A in diameter and 26 A 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 glycerophosphoethanolamine 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.
Hosoda
K
K
Department of Biochemical Sciences, Gunma University.
Ohya
M
M
Kohno
T
T
Maeda
T
T
Endo
S
S
Wakamatsu
K
K
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001430:Bacteriocins; D008246:Lysophospholipids / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010456:Peptides, Cyclic; D011522:Protons
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D008246:Lysophospholipids; D010456:Peptides, Cyclic; D011522:Protons; C008301:lysophosphatidylethanolamine; C000485:cinnamycin