Selective binding of bryostatin analogues to the cysteine rich domains of protein kinase C isozymes.
Designed bryostatin analogues are assayed for binding affinity to individual cysteine rich domains of several protein kinase C (PKC) isozymes. These analogues exhibit significant selectivity for the PKCdelta-C1B peptide in terms of absolute affinity and the PKCdelta-C1A peptide in terms of relative affinity when compared to phorbol-12,13-dibutyrate.
Department of Chemistry, Stanford University, CA 94305-5080, USA.
P A
PA
Wender
B
B
Lippa
C M
CM
Park
K
K
Irie
A
A
Nakahara
H
H
Ohigashi
D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism*; D001667:Binding, Competitive; D054713:Bryostatins; D003545:Cysteine / Q000378:metabolism*; D004789:Enzyme Activation; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007783:Lactones / Q000737:chemistry / Q000378:metabolism*; D018942:Macrolides; D011487:Protein Conformation; D011493:Protein Kinase C / Q000737:chemistry / Q000378:metabolism*; D051745:Protein Kinase C-delta; D014407:Tumor Cells, Cultured
D000970:Antineoplastic Agents; D054713:Bryostatins; D007527:Isoenzymes; D007783:Lactones; D018942:Macrolides; C046785:bryostatin 1; C497258:PRKCD protein, human; D011493:Protein Kinase C; D051745:Protein Kinase C-delta; D003545:Cysteine