1v00

From Proteopedia

Revision as of 16:10, 18 December 2007

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 LAT, MN and CA 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

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