Ito A, Hashimoto T, Hirai M, Takeda T, Shuntoh H, Kuno T, Tanaka C
Department of Pharmacology, Kobe University School of Medicine, Japan.
Biochem Biophys Res Commun. 1989 Sep 29;163(3):1492-7. doi: 10.1016/0006-291x(89)91148-0.
A complementary DNA (cDNA) clone encoding the catalytic subunit of calcineurin (calcineurin A) has been isolated from a rat brain cDNA library. The primary structure of the cDNA consists of 2,337 nucleotides including the entire coding region for 521 amino acids, and the calculated molecular mass is 58,643 Da. The calcineurin A is strikingly homologous to protein phosphatases 1 and 2A, approximately 50% of the amino acids over an internal 250-residue region between residues 78 and 329 being identical. Twenty four amino acid-residue region between residues 391 and 414 shows the consensus structural features for a calmodulin-binding domain. These data suggest that the allosteric character of this chimeric enzyme is generated by gene fusion of two separate protein families.
已从大鼠脑cDNA文库中分离出一个编码钙调神经磷酸酶催化亚基（钙调神经磷酸酶A）的互补DNA（cDNA）克隆。该cDNA的一级结构由2337个核苷酸组成，包括521个氨基酸的完整编码区，计算出的分子量为58643道尔顿。钙调神经磷酸酶A与蛋白磷酸酶1和2A具有显著的同源性，在78至329位残基之间的一个250个残基的内部区域中，约50%的氨基酸是相同的。391至414位残基之间的24个氨基酸残基区域显示出钙调蛋白结合域的共有结构特征。这些数据表明，这种嵌合酶的变构特性是由两个独立蛋白质家族的基因融合产生的。
