A family of mutant proteins related to calmodulin (CaM) has been produced using cDNA constructs in bacterial expression vectors. The new proteins contain amino acid substitutions in Ca2+-binding domains I, II, both I and II, or both II and IV. The calmodulin-like proteins have been characterized with respect to mobility on SDS-polyacrylamide gels, Ca2+-dependent enhancement of tyrosine fluorescence, and abilities to activate the CaM-dependent phosphatase calcineurin. These studies suggest that an intact Ca2+-binding domain II is minimally required for full activation of calcineurin.
No takes yet. Share an insight, caveat, or question.
Hurwitz et al. (1988) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: