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]
Plant beta-galactosidases EC 3.2.1.23 (lactases).
Mammalian latrophilin, the calcium independent receptor of alpha-latrotoxin (CIRL). The galactose-binding lectin domain is not required for alpha-latratoxin binding.[5]
Human latrophilin-1.
Human Latrophilin-2.
Rhamnose-binding lectin (SAL) from catfish (Silurus asotus) eggs. This protein is composed of three tandem repeat domains homologous to the SUEL lectin domain. All cysteine positions of each domain are completely conserved.[2]
The hypothetical B0457.1, F32A7.3A and F32A7.3B proteins from Caenorhabditis elegans.
^ 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. PMID 2001368.
^ 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. PMID 10564781.
^Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF, Ushkaryov YA (August 1997). "Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors". J. Biol. Chem. 272 (34): 21504–8. doi:10.1074/jbc.272.34.21504. PMID 9261169.
^Tateno H, Saneyoshi A, Ogawa T, Muramoto K, Kamiya H, Saneyoshi M (July 1998). "Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily". J. Biol. Chem. 273 (30): 19190–7. doi:10.1074/jbc.273.30.19190. PMID 9668106.
^ abKrasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG (February 1999). "Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants". J. Biol. Chem. 274 (6): 3590–6. doi:10.1074/jbc.274.6.3590. PMID 9920906.
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