Leguminous lectin family Leguminous lectin family In molecular biology, the leguminous lectin family is a family of lectin proteins. It is one of the largest lectin families with more than 70 lectins reported in a review in 1990. Leguminous lectins consist of two or four subunits, each containing one carbohydrate-binding site. The interaction with sugars requires tightly bound calcium and manganese ions. The structural similarities of these lectins are reported by the primary structural analyses and X-ray crystallographic studies. X-ray studies have shown that the folding of the polypeptide chains in the region of the carbohydrate-binding sites is also similar, despite differences in
Alpha-keratin large variation in α-keratin structures found in mammals. α-keratin synthesis begins near focal adhesions on the cell membrane. There, the keratin filament precursors go through a process known as nucleation, where the keratin precursors of dimers and filaments elongate, fuse, and bundles together. As this synthesis is occurring, the keratin filament precursors are transported by actin fibers in the cell towards the nucleus. There, the alpha-keratin intermediate filaments will collect and form networks of structure dictated by the use of the keratin cell as the nucleus simultaneously degrades. However, if necessary, instead of continuing to grow, the keratin complex will