Czurylo E A
Nencki Institute of Experimental Biology PAS, Warszawa, Poland.
Tsitologiia. 2000;42(1):7-18.
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.
本文描述了钙调蛋白在平滑肌细胞中的分布及其体外实验特性。将这些特性与其他调节蛋白以及推测发挥此作用的蛋白质的特性进行比较，结果表明钙调蛋白具有另一种尚未明确的功能。基于现有的实验和理论数据，已尝试对多肽链结构元件的含量及其定位进行定量估算。考虑到钙调蛋白的结构域，提出了所有已知钙调蛋白序列二级结构的通用模型。基于其他蛋白质CH结构域的已知X射线数据，提出了钙调蛋白分子疏水核心的一种可能结构。
