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1SLC

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

Summary for 1SLC
Entry DOI10.2210/pdb1slc/pdb
DescriptorBOVINE 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 Keywordscomplex(lectin-saccharide), complex(lectin-saccharide) complex, complex(lectin/saccharide)
Biological sourceBos taurus (cow)
Total number of polymer chains4
Total formula weight61386.63
Authors
Bourne, Y.,Cambillau, C. (deposition date: 1994-03-12, release date: 1995-01-26, Last modification date: 2024-10-23)
Primary citationBourne, 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: 7773775
DOI: 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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数据于2024-10-30公开中

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