1v00
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Erythrina cristagalli lectin (ECL) is a galactose-specific legume lectin. | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Eukaryota]] | [[Category: Eukaryota]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acharya, K | + | [[Category: Acharya, K R.]] |
| - | [[Category: Chaddock, J | + | [[Category: Chaddock, J A.]] |
[[Category: Natesh, R.]] | [[Category: Natesh, R.]] | ||
[[Category: Thiyagarajan, N.]] | [[Category: Thiyagarajan, N.]] | ||
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[[Category: non-canonical dimer]] | [[Category: non-canonical dimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:09 2008'' |
Revision as of 13:30, 21 February 2008
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ERYTHRINA CRISTAGALLI LECTIN
Overview
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.
About this Structure
1V00 is a Single protein structure of sequence from Eukaryota with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structures of Erythrina cristagalli lectin with bound N-linked oligosaccharide and lactose., Turton K, Natesh R, Thiyagarajan N, Chaddock JA, Acharya KR, Glycobiology. 2004 Oct;14(10):923-9. Epub 2004 Jun 16. PMID:15201215
Page seeded by OCA on Thu Feb 21 15:30:09 2008
Categories: Eukaryota | Single protein | Acharya, K R. | Chaddock, J A. | Natesh, R. | Thiyagarajan, N. | Turton, K. | CA | LAT | MN | Carbohydrate-binding | Lectin | Non-canonical dimer
