2iho

<StructureSection load='2iho' size='340' side='right' caption='[[2iho]], [[Resolution|resolution]] 2.41&Aring;' scene=''>

<table><tr><td colspan='2'>[[2iho]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Marasmius_oreades Marasmius oreades]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IHO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iho OCA], [http://pdbe.org/2iho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iho RCSB], [http://www.ebi.ac.uk/pdbsum/2iho PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/2iho_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 A resolution, in complex with the linear trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.

Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope.,Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:17442345<ref>PMID:17442345</ref>

== References ==

[[Category: Askarieh, G]]

[[Category: Goldstein, I J]]

[[Category: Grahn, E]]

[[Category: Holmner, A]]

[[Category: Krengel, U]]

[[Category: Tateno, H]]

[[Category: Winter, H C]]

[[Category: Sugar binding protein]]