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Specific inhibition of AGC protein kinases by antibodies against C‐terminal epitopes
Author(s) -
Traincard François,
Giacomoni Véronique,
Veron Michel
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.013
Subject(s) - kinase , biochemistry , protein kinase a , epitope , c raf , chemistry , sh3 domain , map2k7 , microbiology and biotechnology , antibody , mitogen activated protein kinase kinase , biology , cyclin dependent kinase 2 , proto oncogene tyrosine protein kinase src , genetics
The sequences contributing to the catalytic site of protein kinases are not all comprised within the highly conserved catalytic core. Thus, in mammalian cAMP‐dependent protein kinase (PKA), the C‐terminal sequence participates in substrate binding. Using synthetic peptides mimicking the FxxF motif present at most C‐termini of AGC kinases, we have raised highly specific antibodies which are potent and specific inhibitors of the catalytic activity of the cognate protein kinase. Taking into account the structure of PKA, these results point to the potential of the C‐terminal region of protein kinases as a target for designing specific protein kinase inhibitors.