Keratin 5 Keratin 5 Keratin 5, also known as KRT5, K5, or CK5, is a protein that is encoded in humans by the "KRT5" gene. It dimerizes with keratin 14 and forms the intermediate filaments (IF) that make up the cytoskeleton of basal epithelial cells. This protein is involved in several diseases including epidermolysis bullosa simplex and breast and lung cancers. Keratin 5, like other members of the keratin family, is an intermediate filament protein. These polypeptides are characterized by a 310 residue central rod domain that consists of four alpha helix segments (helix 1A, 1B, 2A, and 2B) connected by three
Alpha-keratin of most biological importance of alpha-keratin is its structural stability. When exposed to mechanical stress, α-keratin structures can retain their shape and therefore can protect what they surround. Under high tension, alpha-keratin can even change into beta-keratin, a stronger keratin formation that has a secondary structure of beta-pleated sheets. Alpha-keratin tissues also show signs of viscoelasticity, allowing them to both be able to stretch and absorb impact to a degree, though they are not impervious to fracture. Alpha-keratin strength is also affected by water content in the intermediate filament matrix; higher water content decreases the strength and stiffness of the