1PTR

Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester.

(1995) Cell 81: 917-924

• PubMed: 7781068 Search on PubMed
• DOI: https://doi.org/10.1016/0092-8674(95)90011-x
• Primary Citation of Related Structures:  
  1PTQ, 1PTR


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580, USA.