Calponin为一种平滑肌特有的调控蛋白, 分子克隆的证据表明, 它具有两种亚型, α型和β型分别由292和252个氨基酸组成它能与肌动蛋白结合, 抑制肌球蛋白ATP酶活性和平滑肌收缩其与肌动蛋白结合域有38个氨基酸残基(第145~182位), 丝氨酸175在调宁蛋白与肌动蛋白的相互作用中起重要作用, 它还能与钙调蛋白结合, 呈钙依赖性, 其结构域在第52~144位残基调宁蛋白的机能受磷酸化与脱磷酸化的调节.
Calponin is a smooth muscle-specific regulatory protein. The evidences of molecular cloning revealed the existence of 2 isoforms:α and β, composed of 292 and 252 residues respectively. Calponin binds to actin and inhibits actomyosin Mad2+-ATPase activity, thereby smooth muscle contraction. The actin-binding domain of calponin lies in 38 residues (145-182). Ser175 plays a critical role in the interaction of calponin with actin and the inhibition of the ATPase. It also binds to calmodulin in a Ca2+-dependent manner. The calmodulin-binding domain is between residue 52 and 144. Both binding and inhibition of the ATPase can be regulated by phosphorylation and dephosphorylation of calponin.
唐大椿,向继洲,鲁文彤.一种新的平滑肌调控蛋白Calponin[J].生物化学与生物物理进展,1996,23(4):325-329
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