Structural homology between hard alpha-keratin and the intermediate filament proteins desmin and vimentin.
Although it has been assumed that the microfibrils in hard -keratin are members of the class of structures known as intermediate filaments (IF), no firm chemical evidence relating the low-sulfur proteins in hard -keratin to other IF proteins has yet been published. We now present primary sequence data for two components from wool keratin which show striking similarities with two IF proteins, desmin and vimentin. The sequences show marked homology, a heptad repeat and a 9.5-residue periodicity in the linear disposition of the acidic and the basic residues. These data thus provide the first evidence that the low-sulfur proteins in hard -keratin and the other IF proteins do indeed have both a similar structure and a common evolutionary origin.
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003893:Desmin; D005895:Gizzard, Avian / Q000032:analysis; D007381:Intermediate Filament Proteins; D007633:Keratins; D007908:Lens, Crystalline / Q000032:analysis; D013552:Swine; D014746:Vimentin; D014935:Wool
D003893:Desmin; D007381:Intermediate Filament Proteins; D014746:Vimentin; D007633:Keratins