Structure Determination of an Immunopotentiator Peptide, Cinnamycin, Complexed with Lysophosphatidylethanolamine by 1H-NMR1

Overview

Journal J Biochem

Publisher Oxford University Press

Specialty Biochemistry

Date 1996 Feb 1

PMID 8882709

Citations 22

Authors

K Hosoda

M Ohya

T Kohno

T Maeda

S Endo

K Wakamatsu

Affiliations

Soon will be listed here.

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 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.

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