Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins

Abstract

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.