Open AccessThe structure of the B subunit of calcineurin
Author(s) -
AITKEN Alastair,
KLEE Claude B.,
COHEN Philip
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08055.x
Subject(s) - protein subunit , biochemistry , protein primary structure , residue (chemistry) , peptide sequence , calcineurin , calmodulin , chemistry , myristoylation , biology , enzyme , gene , phosphorylation , medicine , surgery , transplantation
The complete primary structure of the B subunit of calcineurin (protein phosphatase 2B) has been determined by automated sequence analysis. The protein consists of a single polypeptide chain of 168 residues, relative molecular mass 19200. The structure shows 35% identity with the sequence of calmodulin and 29% with troponin C. Homology is mainly confined to the regions of the four putative Ca 2+ ‐binding loops. The results demonstrate that the B subunit is a new member of this family of Ca 2+ ‐binding proteins. The N‐terminal glycine residue is blocked with the C 14 ‐saturated fatty acid myristic acid and the first four residues are very similar to those of the catalytic subunit of cyclic‐AMP‐dependent protein kinase which also contains a myristoyl blocking group.