1SLB

X-RAY CRYSTALLOGRAPHY REVEALS CROSSLINKING OF MAMMALIAN LECTIN (GALECTIN-1) BY BIANTENNARY COMPLEX TYPE SACCHARIDES

Summary for 1SLB

• Entry DOI: 10.2210/pdb1slb/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)]alpha-D-mannopyranose, ... (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: 61183.44

Authors

Bourne, Y.,Cambillau, C. (deposition date: 1994-03-12, release date: 1995-01-26, Last modification date: 2024-10-09)

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

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: 7773775
DOI: 10.1038/nsb1294-863

Experimental method

X-RAY DIFFRACTION (2.3 Å)