2dde
From Proteopedia
Structure of cinnamycin complexed with lysophosphatidylethanolamine
Structural highlights
FunctionCINA_STRGV Can act as inhibitor of the enzyme phospholipase A2, and of the angiotensin-converting enzyme. Shows inhibitory activities against herpes simplex virus and immunopotentiating activities. Its antimicrobial activities are not very pronounced. Publication Abstract from PubMedThe 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. Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.,Hosoda K, Ohya M, Kohno T, Maeda T, Endo S, Wakamatsu K J Biochem. 1996 Feb;119(2):226-30. PMID:8882709[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
|
| |||||||||||||||||||
