2iho: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2iho |SIZE=350|CAPTION= <scene name='initialview01'>2iho</scene>, resolution 2.41Å | |PDB= 2iho |SIZE=350|CAPTION= <scene name='initialview01'>2iho</scene>, resolution 2.41Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2iho PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iho RCSB]</span> | |||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
''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 03:44:30 2008'' | ||
Revision as of 03:44, 31 March 2008
| |||||||
| , resolution 2.41Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc
OverviewOverview
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.
About this StructureAbout this Structure
2IHO is a Single protein structure of sequence from Marasmius oreades. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Mar 31 03:44:30 2008