Mastoparan binding induces a structural change affecting both the N-terminal and C-terminal domains of calmodulin. A 113Cd-NMR study.
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 protein- bound 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.
D000595:Amino Acid Sequence; D000818:Animals; D001514:Bee Venoms / Q000378:metabolism*; D001665:Binding Sites; D002104:Cadmium; D002147:Calmodulin / Q000378:metabolism*; D002417:Cattle; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D010455:Peptides; D011487:Protein Conformation / Q000187:drug effects; D014862:Wasp Venoms / Q000378:metabolism*
D001514:Bee Venoms; D002147:Calmodulin; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D014862:Wasp Venoms; D002104:Cadmium; C037500:mastoparan