Journal article
Echinococcus granulosus myophilin - Relationship with protein homologues containing 'calponin-motifs'
RM Martin, NB Chilton, MW Lightowlers, RB Gasser
International Journal for Parasitology | PERGAMON-ELSEVIER SCIENCE LTD | Published : 1997
Abstract
Myophilin, a smooth-muscle protein of the tapeworm Echinococcus granulosus, was recently postulated to be a member of the calponin family of proteins. A detailed genetic analysis revealed that 17 proteins had significant homology with the amino-acid sequence of the N-terminal region of myophilin and/or possessed one or more 'calponin-motifs'. Comparison of the amino-acid sequences of the N-terminus showed that the homologous proteins clustered into distinct groups based on the number of calponin-motifs. The calponin-motif of myophilin was genetically more similar to that present in the muscle protein mp20 of Drosophila melanogaster than to those in any other homologous proteins of vertebrate..
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