Galactose binding lectin domain
{{Infobox protein family
| Symbol = Gal_Lectin
| Name = Gal_Lectin
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| caption = solution structure of the gal_lectin domain of mouse latrophilin-1 gpcr
| Pfam = PF02140
| Pfam_clan =
| InterPro = IPR000922
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
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.{{cite journal |vauthors=Ozeki Y, Matsui T, Suzuki M, Titani K | title = Amino acid sequence and molecular characterization of a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs | journal = Biochemistry | volume = 30 | issue = 9 | pages = 2391–4 |date=March 1991 | pmid = 2001368 | doi = 10.1021/bi00223a014 }} 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.{{cite journal |vauthors=Hosono M, Ishikawa K, Mineki R, Murayama K, Numata C, Ogawa Y, Takayanagi Y, Nitta K | title = Tandem repeat structure of rhamnose-binding lectin from catfish (Silurus asotus) eggs | journal = Biochim. Biophys. Acta | volume = 1472 | issue = 3 | pages = 668–75 |date=November 1999 | pmid = 10564781 | doi = 10.1016/S0304-4165(99)00185-3}} 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:{{cite journal |vauthors=Lelianova VG, Davletov BA, Sterling A, Rahman MA, Grishin EV, Totty NF, Ushkaryov YA | title = Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin family of G protein-coupled receptors | journal = J. Biol. Chem. | volume = 272 | issue = 34 | pages = 21504–8 |date=August 1997 | pmid = 9261169 | doi = 10.1074/jbc.272.34.21504| doi-access = free }}{{cite journal |vauthors=Tateno H, Saneyoshi A, Ogawa T, Muramoto K, Kamiya H, Saneyoshi M | title = Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily | journal = J. Biol. Chem. | volume = 273 | issue = 30 | pages = 19190–7 |date=July 1998 | pmid = 9668106 | doi = 10.1074/jbc.273.30.19190| doi-access = free }}{{cite journal |vauthors=Krasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG | title = Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants | journal = J. Biol. Chem. | volume = 274 | issue = 6 | pages = 3590–6 |date=February 1999 | pmid = 9920906 | doi = 10.1074/jbc.274.6.3590| doi-access = free }}
- Plant beta-galactosidases {{EC number|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.
- 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.
- The hypothetical B0457.1, F32A7.3A and F32A7.3B proteins from Caenorhabditis elegans.