Galactose binding lectin domain Galactose binding lectin domain In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin ("Anthocidaris crassispina") eggs, SUEL. This lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring
Keratin 5 heterodimers are formed between specific pairs of type I (acidic) and type II (basic) keratin. K5, a type II keratin, pairs with the type I keratin K14. The coiled-coil dimers undergo stepwise assembly and combine in an antiparallel manner, forming end-to-end interactions with other coiled-coils to form large 10 nm intermediate filaments. Keratin 5 (and K14) are expressed primarily in basal keratinocytes in the epidermis, specifically in the stratified epithelium lining the skin and digestive tract. Keratin intermediate filaments make up the cytoskeletal scaffold within epithelial cells, which contributes to the cell architecture and provides the cells with the ability