[Calponin: biological, chemical and structural properties].
Calponin distribution in smooth muscle cells and its properties in experiments in vitro are described. A comparison of these properties with those of other regulatory proteins and of proteins presumed to play this role suggest that calponin has another, yet unknown function. On the basis of existing experimental and theoretical data, an attempt has been made to quantitatively estimate the content of structural elements of the polypeptide chain and their localization. With consideration of the structural calponin domains, a general model of the secondary structure of all known calponin sequences is suggested. Based on the known roentgenographic data of the CH-domain of other proteins a possible organization of the calponin molecule hydrophobic core has been proposed.
Czurylo
E A
EA
Nencki Institute of Experimental Biology PAS, Warszawa, Poland. eczurylo@nencki.gov.pl
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D006801:Humans; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000737:chemistry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D000096985:Calponins
D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D000096985:Calponins