Mastoparan binding induces a structural change affecting both the N‐terminal and C‐terminal domains of calmodulin

FEBS Letters

Drakenberg, Torbjörn¹  Linse, Sara¹  Forsén, Sture¹ 

[1] Physical Chemistry 2, Chemical Center, PO Box 124, 221 00 Lund, Sweden

关键词: Mastoparan;    Calmodulin;    Peptide-calmodulin interaction;    Calmodulin-binding peptide;    113Cd-NMR;    ACTH;    adrenocorticotropic hormone;    9AC;    9-anthroylcholine;    ANS;    8-anilinonaphthalenesulfonate;    TNS;    2-p-toluidinylnaphthalene-6-sulfonate;   

DOI  :  10.1016/0014-5793(86)81217-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹¹³Cd-NMR studies of solutions of cadmium-loaded calmodulin (Cd₄CaM) and the tetradecapeptide mastoparan in different ratios show that mastoparan binds to Cd₄CaM 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 Cd₄CaM 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.

【 授权许可】

Unknown