Evaluation of series of isobenzofuranone dimers as PKCalpha ligands: implication for the distance between the two ligand binding sites.
Protein kinase C (PKC) is a family of enzymes, which play important roles in intracellular signal transduction. To examine the distance between the two ligand binding sites (C1A and C1B) of PKC, we designed and synthesized two series of isobenzofuranone dimers. Peak binding activities were observed for the C3-acyl chain dimers having a C10-C12 linker and for the C7 dimers having a C14-C16.
Baba
Yoshiyasu
Y
Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
Mayumi
Satoshi
S
Hirai
Go
G
Kawasaki
Hidekazu
H
Ogoshi
Yosuke
Y
Yanagisawa
Takeshi
T
Hashimoto
Yuichi
Y
Sodeoka
Mikiko
M
D001572:Benzofurans / Q000138:chemical synthesis / Q000494:pharmacology*; D001665:Binding Sites; D019281:Dimerization; D004305:Dose-Response Relationship, Drug; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D011493:Protein Kinase C / Q000037:antagonists & inhibitors* / Q000737:chemistry; D051571:Protein Kinase C-alpha; D013329:Structure-Activity Relationship
D001572:Benzofurans; D004791:Enzyme Inhibitors; D008024:Ligands; C496628:PRKCA protein, human; D011493:Protein Kinase C; D051571:Protein Kinase C-alpha