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  • Title: Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A.
    Author: Noguchi M, Izumi Y, Yoshino H.
    Journal: FEBS Lett; 2004 Aug 27; 573(1-3):121-6. PubMed ID: 15327986.
    Abstract:
    Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391-414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385-414, 380-414 and 374-414 of calcineurin A were used for this aim. The X-ray data are consistent with the fact that calmodulin binds all three peptides with or without Ca2+. Without Ca2+, the whole peptide including acid residues interacts with dumbbell shaped calmodulin, while the acid region is extruded from globular shaped calmodulin with Ca2+. Consequently, a conformation of sequence 374-414 in calcineurin might be changed by Ca2+-signal via calmodulin, suggesting the consequence of this region with acid residues in the full activation mechanism of calcineurin by Ca2+-bound calmodulin.
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