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1iuc

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(New page: 200px<br /><applet load="1iuc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iuc, resolution 2.24&Aring;" /> '''Fucose-specific lect...)
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[[Image:1iuc.jpg|left|200px]]<br /><applet load="1iuc" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1iuc.jpg|left|200px]]<br /><applet load="1iuc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iuc, resolution 2.24&Aring;" />
caption="1iuc, resolution 2.24&Aring;" />
'''Fucose-specific lectin from Aleuria aurantia with three ligands'''<br />
'''Fucose-specific lectin from Aleuria aurantia with three ligands'''<br />
==Overview==
==Overview==
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Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely, used as a specific probe for fucose. Fucosylated sugars often play pivotal, roles in many cellular processes. We have determined the crystal structure, of AAL at 2.24 A resolution in complex with only three fucose molecules in, its five sugar binding sites of a six-fold beta-propeller structure. Very, recently, the structure of AAL has been independently determined, showing, that all the five binding sites were occupied by fucose molecules, [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]., Stabilization of the arginine conformation bound to fucose molecules plays, an essential role in generating the difference in the affinity in the five, binding sites. Binding models with a couple of saccharides based on, biochemical assays suggest that hydrophobic contacts also play important, roles in AAL recognizing its ligand.
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Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand.
==About this Structure==
==About this Structure==
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1IUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aleuria_aurantia Aleuria aurantia] with FUL, FUC and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IUC OCA].
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1IUC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aleuria_aurantia Aleuria aurantia] with <scene name='pdbligand=FUL:'>FUL</scene>, <scene name='pdbligand=FUC:'>FUC</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUC OCA].
==Reference==
==Reference==
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[[Category: Miki, K.]]
[[Category: Miki, K.]]
[[Category: Nagata, Y.]]
[[Category: Nagata, Y.]]
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[[Category: Peapus, D.H.]]
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[[Category: Peapus, D H.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: FUC]]
[[Category: FUC]]
[[Category: FUL]]
[[Category: FUL]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:40:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:43 2008''

Revision as of 11:15, 21 February 2008


1iuc, resolution 2.24Å

Drag the structure with the mouse to rotate

Fucose-specific lectin from Aleuria aurantia with three ligands

Overview

Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand.

About this Structure

1IUC is a Single protein structure of sequence from Aleuria aurantia with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of fucose-specific lectin from Aleuria aurantia binding ligands at three of its five sugar recognition sites., Fujihashi M, Peapus DH, Kamiya N, Nagata Y, Miki K, Biochemistry. 2003 Sep 30;42(38):11093-9. PMID:14503859

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