2fmd
From Proteopedia
(New page: 200px<br /><applet load="2fmd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fmd, resolution 1.9Å" /> '''Structural basis of c...) |
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| - | [[Image:2fmd.gif|left|200px]]<br /><applet load="2fmd" size=" | + | [[Image:2fmd.gif|left|200px]]<br /><applet load="2fmd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fmd, resolution 1.9Å" /> | caption="2fmd, resolution 1.9Å" /> | ||
'''Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin'''<br /> | '''Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the seed lectin from the tropical legume | + | The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219. |
==About this Structure== | ==About this Structure== | ||
| - | 2FMD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bowringia_mildbraedii Bowringia mildbraedii] with CA and MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FMD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bowringia_mildbraedii Bowringia mildbraedii] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-carbohydrate complex]] | [[Category: protein-carbohydrate complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:52 2008'' |
Revision as of 15:22, 21 February 2008
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Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin
Overview
The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219.
About this Structure
2FMD is a Single protein structure of sequence from Bowringia mildbraedii with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii., Buts L, Garcia-Pino A, Wyns L, Loris R, Glycobiology. 2006 Jul;16(7):635-40. Epub 2006 Mar 27. PMID:16567368
Page seeded by OCA on Thu Feb 21 17:22:52 2008
