Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKC delta.

Journal of medicinal chemistry - 26 Jul 2007

Choi Yongseok, Pu Yongmei, Peach Megan L, Kang Ji-Hye, Lewin Nancy E, Sigano Dina M, Garfield Susan H, Blumberg Peter M, Marquez Victor E

Abstract excerpt

Diacylglycerol (DAG) lactones have provided a powerful platform for structural exploration of the interactions between ligands and the C1 domains of protein kinase C (PKC). In this study, we report that DAG-dioxolanones, novel derivatives of DAG-lactones, exploit an additional point of contact (glutamine 27) in their binding with the C1b domain of PKC delta. Mutation of this point of contact to glutamate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CHO Cells
Share to Cricetulus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Diglycerides

Share to Glutamine

Share to Lactones

Share to Molecular Conformation

Share to Protein Kinase C-delta

Share to Stereoisomerism

Source

Identifiers

PMID: 17591763
DOI: 10.1021/jm0702579

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKC delta.PMID 17591763Read ↗

Role of hydrophobic residues in the C1b domain of protein kinase C delta on ligand and phospholipid interactions.Semantic proximity Read ↗

Catalytic activity and acyl-chain selectivity of diacylglycerol kinase ɛ are modulated by residues in and near the lipoxygenase-like motif.Semantic proximity Read ↗

Characterization of the differential roles of the twin C1a and C1b domains of protein kinase C-delta.Semantic proximity Read ↗

PKC epsilon has an alcohol-binding site in its second cysteine-rich regulatory domain.Semantic proximity Read ↗

The origin of C1A-C2 interdomain interactions in protein kinase Calpha.Semantic proximity Read ↗

Differential protein kinase C ligand regulation detected in vivo by a phenotypic yeast assay.Semantic proximity Read ↗

Diacylglycerol kinase gamma is one of the specific receptors of tumor-promoting phorbol esters.Semantic proximity Read ↗

Probing the determinants of diacylglycerol binding affinity in the C1B domain of protein kinase Cα.Semantic proximity Read ↗

Crystal structure and allosteric activation of protein kinase C βII.Semantic proximity Read ↗

Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.Semantic proximity Read ↗

A cannabinoid receptor 1 mutation proximal to the DRY motif results in constitutive activity and reveals intramolecular interactions involved in receptor activation.Semantic proximity Read ↗

GDAP1 binds 4-hydroxynonenal, the toxic end-product of lipid peroxidation, using its GST-like binding pocketSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.