2dde | pdb_00002dde

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Structure of cinnamycin complexed with lysophosphatidylethanolamine

File:2dde.gif


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2dde
Ligands: LSP
Coordinates: save as pdb, mmCIF, xml



Overview

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.

About this Structure

2DDE is a Single protein structure of sequence from Streptomyces griseoverticillatus. Full crystallographic information is available from OCA.

Reference

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

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