PROTEIN KINASE C DELTA CYS2 DOMAIN

File:1ptq.gif


1ptq, resolution 1.95Å

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OverviewOverview

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.

About this StructureAbout this Structure

1PTQ is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester., Zhang G, Kazanietz MG, Blumberg PM, Hurley JH, Cell. 1995 Jun 16;81(6):917-24. PMID:7781068

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