1SLC
X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES
Summary for 1SLC
Entry DOI | 10.2210/pdb1slc/pdb |
Descriptor | BOVINE GALECTIN-1, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | complex(lectin-saccharide), complex(lectin-saccharide) complex, complex(lectin/saccharide) |
Biological source | Bos taurus (cow) |
Total number of polymer chains | 4 |
Total formula weight | 61386.63 |
Authors | Bourne, Y.,Cambillau, C. (deposition date: 1994-03-12, release date: 1995-01-26, Last modification date: 2024-10-23) |
Primary citation | Bourne, Y.,Bolgiano, B.,Liao, D.I.,Strecker, G.,Cantau, P.,Herzberg, O.,Feizi, T.,Cambillau, C. Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nat.Struct.Biol., 1:863-870, 1994 Cited by PubMed Abstract: Galectins are beta-galactoside-binding proteins that occur intra- and extracellularly in many animal tissues. They have been proposed to form networks of glycoconjugates on the cell surface, where they may modulate various cell response pathways such as growth, activation and adhesion. The high resolution X-ray crystallographic analyses of three crystal forms of bovine galectin-1 in complex with biantennary saccharides of N-acetyllactosamine type reveal infinite chains of lectin dimers cross-linked through N-acetyllactosamine units located at the end of the oligosaccharide antenna. The oligosaccharide adopts a different low energy conformation in each of the three crystal forms. PubMed: 7773775DOI: 10.1038/nsb1294-863 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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