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Article

Characterization of phospho-(tyrosine)-mimetic calmodulin mutants.

PloS one - 1 Jan 2015

Stateva Silviya R, Salas Valentina, Benaim Gustavo, Menéndez Margarita, Solís Dolores, Villalobo Antonio

Abstract excerpt

Calmodulin (CaM) phosphorylated at different serine/threonine and tyrosine residues is known to exert differential regulatory effects on a variety of CaM-binding enzymes as compared to non-phosphorylated CaM. In this report we describe the preparation and characterization of a series of phospho-(Y)-mimetic CaM mutants in which either one or the two tyrosine residues present in CaM (Y99 and Y138) were substituted...

Topics

Amino Acid Substitution
Animals
Calmodulin
Cattle
Chemical Phenomena
Cyclic Nucleotide Phosphodiesterases, Type 1
Mutation
Nitric Oxide Synthase Type III
Phosphotyrosine
Protein Stability
Rats

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Identifiers

PMID: 25830911
DOI: 10.1371/journal.pone.0120798
PMCID: PMC4382182

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