| Literature DB >> 2844597 |
M Y Hurwitz1, J A Putkey, C B Klee, A R Means.
Abstract
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.Entities:
Mesh：
Substances：
Year: 1988 PMID： 2844597 DOI： 10.1016/0014-5793(88)80230-8
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124