Three-dimensional modelling of interchain sequence similarities and differences in the coiled-coil segments of keratin intermediate filament heterodimers highlight features important in assembly

The study explored the structural and functional rationale for the preference of heterodimer structures over homodimers in keratin intermediate filaments (IF). Using three-dimensional modeling of coiled-coil segments, the research highlighted the importance of charged and apolar residue distributions in keratin Type I/Type II heterodimers. The study found that heterodimers offer greater specificity and structural advantages, which are crucial for the molecular reorganization of keratins in different environments. This work provided new insights into the spatial features of keratin heterodimers, contributing to the understanding of their assembly and function.