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.[1] 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.[1][2] L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure.
A cysteine-rich domain (the galactose binding lectin domain) homologous to the SUEL protein has been identified in the following proteins:[3][4][5]
^ abOzeki Y, Matsui T, Suzuki M, Titani K (March 1991). "Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs". Biochemistry. 30 (9): 2391–4. doi:10.1021/bi00223a014. PMID2001368.
^ abHosono M, Ishikawa K, Mineki R, Murayama K, Numata C, Ogawa Y, Takayanagi Y, Nitta K (November 1999). "Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs". Biochim. Biophys. Acta. 1472 (3): 668–75. doi:10.1016/S0304-4165(99)00185-3. PMID10564781.