Motifs of the caldesmon family.
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.
Czuryło
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EA
Nencki Institute of Experimental Biology, Department of Muscle Biochemistry, Warszawa, Poland. eczurylo@nencki.gov.pl
D000199:Actins / Q000737:chemistry; D000465:Algorithms; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000737:chemistry; D002148:Calmodulin-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000166:cytology; D009218:Myosins / Q000737:chemistry; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012984:Software; D014335:Tropomyosin / Q000737:chemistry
D000199:Actins; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D020033:Protein Isoforms; D014335:Tropomyosin; D009218:Myosins