2eig: Difference between revisions

Revision as of 00:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2eig.png

Template:STRUCTURE 2eig

Lotus tetragonolobus seed lectin (Isoform)Lotus tetragonolobus seed lectin (Isoform)

Template:ABSTRACT PUBMED 18068379

About this StructureAbout this Structure

2EIG is a Single protein structure of sequence from Lotus tetragonolobus. Full crystallographic information is available from OCA.

ReferenceReference

Identification of a new quaternary association for legume lectins., Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr, J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:18068379

Page seeded by OCA on Mon Jul 28 00:40:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Lotus tetragonolobus seed lectin (Isoform)'''
+===Lotus tetragonolobus seed lectin (Isoform)===
-==Overview==
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-Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.
+The line below this paragraph, {{ABSTRACT_PUBMED_18068379}}, adds the Publication Abstract to the page
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 [[Category: N-acetyl-d-glucosamine]]
 [[Category: Sugar binding protein]]
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