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Protein Engineering, Vol 11, 803-810, Copyright © 1998 by Oxford University Press

ARTICLES

The interaction of myristylated peptides with the catalytic domain of protein kinase C revealed by their sequence palindromy and the identification of a myristyl binding site

A Zaliani, M Pinori, HL Ball, G DiGregorio, P Cremonesi and P Mascagni
Italfarmaco Research Centre, Milan, Italy.

Using a model of the enzyme structure and the results from a series of free and myristylated peptides, we provide evidence that peptides corresponding to the pseudosubstrate sequence of protein kinase C bind to the enzyme substrate binding site in an essentially extended conformation. This and the nearly symmetrical location of positive charges around the substrate phosphoritable site allow the peptide to bind to the enzyme in either an N-to-C orientation or its C-to-N opposite orientation. The latter is favoured by a change in residue chirality or when the peptide bears a myristoyl chain at its N- terminus. A myristyl binding site was also identified in the enzyme structure and its location in a region proximal to the C-terminal residue of pseudosubstrate bound in the N-to-C direction suggested that C-myristylation of peptide substrates should be more effective than N- myristoylation in antagonizing the enzyme. A peptide (H-RFARKGALRQKN- CONH-Myr) which contains the myristyl chain covalently linked to the C- terminal residue of the pseudosubstrate was thus made and shown to be a potent inhibitor of the histone kinase reaction of protein kinase C and the phosphorylation of p47 in intact cells.
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