Parry D A, Conway J F, Steinert P M
Biochem J. 1986 Aug 15;238(1):305-8. doi: 10.1042/bj2380305.
Analysis of the amino acid sequences of lamins A and C has revealed that each chain has an almost continuous heptad-containing coiled-coil domain containing structural regularities in the linear disposition of the acidic and the basic residues. The data suggest that the lamin molecules are two-stranded ropes, that the two chains are parallel to one another and in axial register, and that the molecules aggregate in vivo through periodic ionic interactions. These results indicate that significant changes in stability of the nuclear envelope may be achieved between interphase and mitosis through changes in the degree of phosphorylation of the lamin proteins.
对核纤层蛋白A和C的氨基酸序列分析表明，每条链都有一个几乎连续的含七肽的卷曲螺旋结构域，在酸性和碱性残基的线性排列中包含结构规律。数据表明，核纤层蛋白分子是双链绳索，两条链相互平行且轴向对齐，并且分子在体内通过周期性离子相互作用聚集。这些结果表明，通过改变核纤层蛋白的磷酸化程度，在间期和有丝分裂之间可能实现核膜稳定性的显著变化。
