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Motifs of the caldesmon family.
Author(s) -
Edward A. Czuryło
Publication year - 2000
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2000_3955
Subject(s) - caldesmon , function (biology) , gene , conserved sequence , sequence (biology) , biology , chemistry , computational biology , microbiology and biotechnology , genetics , peptide sequence , biochemistry , calmodulin , enzyme
Seven highly conserved regions were found in caldesmon molecules from various sources using the multiple sequence alignment method. Their localization coincides with regions where the binding sites to other proteins were postulated. Less conserved and highly divergent regions of the sequences are described as well. These results could refine the planning of caldesmon gene manipulations and accelerate the precise localization of binding sites in the caldesmon molecule and, as a consequence, this could help to elucidate its function in smooth muscle contraction.

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