Abstract:
: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 Arg6, Gln7, or Ala9 by other amino acid residues produced a marked increase in the IC50 value. Leu4 and Val10 were also sensitive to replacement, but some hydrophobic amino acids could substitute for these residues. Although replacement of Ala3, Glu8, Ala12, and Leu13 by other residues produced no significant increase in the IC50, the substitution of Lys for Ala3 decreased the IC50. An AIP analog (KKKLRRQEAFDAY), in which Ala3 and Val10 were replaced with Lys and Phe, respectively, showed an IC50 value as low as 4 nM, suggesting that it is a useful tool for studying the physiological roles of CaMKII.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ishida A,Shigeri Y,Tatsu Y,Uegaki K,Kameshita I,Okuno S,Kitani T,Yumoto N,Fujisawa Hdoi
10.1016/s0014-5793(98)00405-0subject
Has Abstractpub_date
1998-05-01 00:00:00pages
115-8issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00405-0journal_volume
427pub_type
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