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Article

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

The Journal of biological chemistry - 1 Jun 2001

Wang Q J, Fang T W, Nacro K, Marquez V E, Wang S, Blumberg P M

Abstract excerpt

The C1 domains of conventional and novel protein kinase C (PKC) isoforms bind diacylglycerol and phorbol esters with high affinity. Highly conserved hydrophobic residues at or near the rim of the binding cleft in the second cysteine-rich domain of PKC-delta (PKC-deltaC1b) were mutated to probe their roles in ligand recognition and lipid interaction. [(3)H]Phorbol 12,13-dibutyrate (PDBu) binding was carried out...

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Identifiers

PMID: 11278612
DOI: 10.1074/jbc.M010089200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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