Keratin protein domains

Keratin protein domains form the tripartite structure of keratins—head, central rod (with coiled-coil subdomains 1A, 1B, 2A, 2B, and linkers L1, L12, L2), and tail—that enable these type I and type II intermediate filament proteins to assemble into 10-nm filaments providing cytoskeletal integrity in epithelial tissues like skin, hair, and nails.[1][2][3] The rod domain drives dimerization and higher-order filament formation through parallel heterodimer coiled-coils, while variable head and tail domains facilitate interactions, compaction, and non-mechanical roles such as signaling.[1][5][9] Mutations disrupting domain assembly cause fragility disorders like epidermolysis bullosa.[9] No drugs directly target these domains therapeutically; research focuses on structural biology rather than pharmacology.[1][2] Keratins are not receptors or enzymes but structural scaffolds essential for epithelial barrier function.[2][5]

Other names

Keratin subdomainshead domainrod domain (1A, L1, 1B, L12, 2A, L2, 2B)tail domaintri-domain structure