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Mastoparan binding induces a structural change affecting both the N‐terminal and C‐terminal domains of calmodulin
Author(s) -
Linse Sara,
Drakenberg Torbjörn,
Forsén Sture
Publication year - 1986
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 - 10.1016/0014-5793(86)81217-0
Subject(s) - mastoparan , calmodulin , chemistry , binding protein , biophysics , plasma protein binding , biochemistry , terminal (telecommunication) , stereochemistry , g protein , biology , receptor , gene , enzyme , telecommunications , computer science
113 Cd‐NMR studies of solutions of cadmium‐loaded calmodulin (Cd 4 CaM) and the tetradecapeptide mastoparan in different ratios show that mastoparan binds to Cd 4 CaM with high affinity. The off‐rate of proteinbound mastoparan is found to be 40 s −1 or less. The binding of one molecule of mastoparan to Cd 4 CaM is observed to affect all four metal‐binding sites, indicating that both the N‐terminal and C‐terminal globular domains of the protein undergo conformational changes.