Recombinant M. musculus CYS2 Activator Binding Domain Complexed with Phorbol Ester

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Protein kinase Cs (PKCs) are a ubiquitous family of regulatory enzymes that associate with membranes and are activated by diacylglycerol or tumor-promoting agonists such as phorbol esters. The structure of the second activator-binding domain of PKC delta has been determined in complex with phorbol 13-acetate, which binds in a groove between two pulled-apart beta strands at the tip of the domain. The C3, C4, and C20 phorbol oxygens form hydrogen bonds with main-chain groups whose orientation is controlled by a set of highly conserved residues. Phorbol binding caps the groove and forms a contiguous hydrophobic surface covering one-third of the domain, explaining how the activator promotes insertion of PKC into membranes.


[1] Zhang G; Kazanietz MG; Blumberg PM; Hurley JH (1995) Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell 81: 917. [

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Last modified Wednesday, 30 July 1997 by Phil Bourne