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N‐terminal domain of dystrophin
Author(s) -
Bonet-Kerrache Armelle,
Fabbrizio Eric,
Mornet Dominique
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01162-1
Subject(s) - dystrophin , calmodulin , utrophin , chemistry , calcium binding protein , actin , binding domain , microbiology and biotechnology , domain (mathematical analysis) , calcium , recombinant dna , biology , biochemistry , biophysics , binding site , enzyme , gene , organic chemistry , mathematical analysis , mathematics
Contro‐versial experiments have been published on calmodulin binding of dystrophin. In this study, we used recombinant proteins and the techniques of affinity chromatography and ELISA to show that the N‐terminal part of dystrophin binds calmodulin specifically in a calcium‐dependent manner. The calcium‐dependent interaction of calmodulin and dystrophin does not directly regulate binding of actin to dystrophin, but may regulate dystrophin interactions with other associated proteins.