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Critical amino acid residues of AIP, a highly specific inhibitory peptide of calmodulin‐dependent protein kinase II
Author(s) -
Ishida Atsuhiko,
Shigeri Yasushi,
Tatsu Yoshiro,
Uegaki Koichi,
Kameshita Isamu,
Okuno Sachiko,
Kitani Takako,
Yumoto Noboru,
Fujisawa Hitoshi
Publication year - 1998
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/s0014-5793(98)00405-0
Subject(s) - chemistry , calmodulin , peptide , amino acid , amino acid residue , biochemistry , protein kinase a , kinase , peptide sequence , stereochemistry , enzyme , gene
The importance of the individual amino acid residues of AIP (KKALRRQEAVDAL), a highly specific inhibitor of calmodulin‐dependent protein kinase II (CaMKII), was studied. Replacement of Arg 6 , Gln 7 , or Ala 9 by other amino acid residues produced a marked increase in the IC 50 value. Leu 4 and Val 10 were also sensitive to replacement, but some hydrophobic amino acids could substitute for these residues. Although replacement of Ala 3 , Glu 8 , Ala 12 , and Leu 13 by other residues produced no significant increase in the IC 50 , the substitution of Lys for Ala 3 decreased the IC 50 . An AIP analog (KK LRRQEA DAY), in which Ala 3 and Val 10 were replaced with Lys and Phe, respectively, showed an IC 50 value as low as 4 nM, suggesting that it is a useful tool for studying the physiological roles of CaMKII.