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PDBsum entry 1v00
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Sugar binding protein
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PDB id
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1v00
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of erythrina cristagalli lectin with bound n-Linked oligosaccharide and lactose.
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Authors
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K.Turton,
R.Natesh,
N.Thiyagarajan,
J.A.Chaddock,
K.R.Acharya.
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Ref.
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Glycobiology, 2004,
14,
923-929.
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PubMed id
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Abstract
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Erythrina cristagalli lectin (ECL) is a galactose-specific legume lectin.
Although its biological function in the legume is unknown, ECL exhibits
hemagglutinating activity in vitro and is mitogenic for T lymphocytes. In
addition, it has been recently shown that ECL forms a novel conjugate when
coupled to a catalytically active derivative of the type A neurotoxin from
Clostridium botulinum, thus providing a therapeutic potential. ECL is
biologically active as a dimer in which each protomer contains a functional
carbohydrate-combining site. The crystal structure of native ECL was recently
reported in complex with lactose and 2'-fucosyllactose. ECL protomers adopt the
legume lectin fold but form non-canonical dimers via the handshake motif as was
previously observed for Erythrina corallodendron lectin. Here we report the
crystal structures of native and recombinant forms of the lectin in three new
crystal forms, both unliganded and in complex with lactose. For the first time,
the detailed structure of the glycosylated hexasaccharide for native ECL has
been elucidated. The structure also shows that in the crystal lattice the
glycosylation site and the carbohydrate binding site are involved in
intermolecular contacts through water-mediated interactions.
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