| Gal_Lectin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Gal_Lectin | ||||||||
| Pfam | PF02140 | ||||||||
| InterPro | IPR000922 | ||||||||
| |||||||||
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.
References
- ^ a b Ozeki 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.
- ^ a b Hosono 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.
- ^ a b Krasnoperov 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.
| Gal_Lectin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Gal_Lectin | ||||||||
| Pfam | PF02140 | ||||||||
| InterPro | IPR000922 | ||||||||
| |||||||||
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.
References
- ^ a b Ozeki 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.
- ^ a b Hosono 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.
- ^ a b Krasnoperov 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.