1v00
From Proteopedia
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|PDB= 1v00 |SIZE=350|CAPTION= <scene name='initialview01'>1v00</scene>, resolution 1.70Å | |PDB= 1v00 |SIZE=350|CAPTION= <scene name='initialview01'>1v00</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LAT:LACTOSE'>LAT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v00 OCA], [http://www.ebi.ac.uk/pdbsum/1v00 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v00 RCSB]</span> | ||
}} | }} | ||
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[[Category: Thiyagarajan, N.]] | [[Category: Thiyagarajan, N.]] | ||
[[Category: Turton, K.]] | [[Category: Turton, K.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: LAT]] | ||
| - | [[Category: MN]] | ||
[[Category: carbohydrate-binding]] | [[Category: carbohydrate-binding]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
[[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 Mon Mar 31 00:17:43 2008'' |
Revision as of 21:17, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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