Galactose binding lectin domain structure. A cysteine-rich domain (the galactose binding lectin domain) homologous to the SUEL protein has been identified in the following proteins: 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
Alpha-keratin disassemble into non-filamentous keratin precursors that can diffuse throughout the cell cytoplasm. These keratin filaments will be able to be used in future keratin synthesis, either to re-organize the final structure or create a different keratin complex. When the cell has been filled with the correct keratin and structured correctly, it undergoes keratin stabilization and dies, a form of programmed cell death. This results in a fully matured, non-vascular keratin cell. These fully matured, or cornified, alpha-keratin cells are the main components of hair, the outer layer of nails and horns, and the epidermis layer of the skin. The property