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1PTR

PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE

Summary for 1PTR
Entry DOI10.2210/pdb1ptr/pdb
DescriptorPROTEIN KINASE C DELTA TYPE, ZINC ION, 13-ACETYLPHORBOL (3 entities in total)
Functional Keywordsphosphotransferase
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm (By similarity): P28867
Total number of polymer chains1
Total formula weight6349.14
Authors
Zhang, G.,Hurley, J.H. (deposition date: 1995-05-11, release date: 1995-07-31, Last modification date: 2024-02-14)
Primary citationZhang, 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: 7781068
DOI: 10.1016/0092-8674(95)90011-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2025-10-01公开中

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