1PTQ
PROTEIN KINASE C DELTA CYS2 DOMAIN
Summary for 1PTQ
Entry DOI | 10.2210/pdb1ptq/pdb |
Descriptor | PROTEIN KINASE C DELTA TYPE, ZINC ION (2 entities in total) |
Functional Keywords | phosphotransferase |
Biological source | Mus musculus (house mouse) |
Cellular location | Cytoplasm (By similarity): P28867 |
Total number of polymer chains | 1 |
Total formula weight | 5942.67 |
Authors | Zhang, G.,Hurley, J.H. (deposition date: 1995-05-11, release date: 1995-07-31, Last modification date: 2024-02-14) |
Primary citation | Zhang, G.,Kazanietz, M.G.,Blumberg, P.M.,Hurley, J.H. Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester. Cell(Cambridge,Mass.), 81:917-924, 1995 Cited by 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. PubMed: 7781068DOI: 10.1016/0092-8674(95)90011-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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