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
Myosin light chain nodes to migrate into inflammatory sites in an S1PR1-dependent manner." The proposed mechanisms of action of CD69/Myl9/12 system are related to the regulation of airway inflammatory processes and thus can prove to be a novel therapeutic target for chronic inflammatory diseases, in general . Myosin light chain A myosin light chain is a light chain (small polypeptide subunit) of myosin. Myosin light chains were discovered by Chinese biochemist Cao Tianqin (Tien-chin Tsao) when he was a graduate student at the University of Cambridge in England. Structurally, myosin light chains belong to the EF-hand family, a large family of Ca- binding