Abstract
Nuclear mitotic apparatus protein (NuMA), also known as centrophilin, has been shown in previous work to contain a centrally located sequence of length 1485 residues that has both a heptad substructure and a high propensity for alpha-helix formation. Further analysis of this sequence here has revealed that NuMA will form a two-stranded coiled-coil structure with multiple (18) points at which the conformation is interrupted either by proline-containing segments or by discontinuities in the phasing of the heptad substructure. It has also been shown that the two chains will be parallel (rather than antiparallel), that they will lie in axial register, and that this arrangement will be stabilized by a large number of interchain ionic interactions. Interestingly the coiled-coil rod domain is also shown to lack any significant long-range periodicity in the linear distribution of either its acidic or its basic residues. Hence there is no direct evidence from the sequence data that NuMA molecules will aggregate to form closely packed filaments within nuclear space.