1iuc: Difference between revisions
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==Fucose-specific lectin from Aleuria aurantia with three ligands== | |||
<StructureSection load='1iuc' size='340' side='right'caption='[[1iuc]], [[Resolution|resolution]] 2.24Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iuc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aleuria_aurantia Aleuria aurantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iuc OCA], [https://pdbe.org/1iuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iuc RCSB], [https://www.ebi.ac.uk/pdbsum/1iuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iuc ProSAT], [https://www.topsan.org/Proteins/RSGI/1iuc TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LECF_ALEAU LECF_ALEAU] Might have a role in the differentiation of cells. Binds L-fucose. | |||
== Evolutionary Conservation == | |||
== | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/1iuc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/main_output.php?pdb_ID=1iuc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:14503859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1iuc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aleuria aurantia]] | [[Category: Aleuria aurantia]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fujihashi | [[Category: Fujihashi M]] | ||
[[Category: Kamiya | [[Category: Kamiya N]] | ||
[[Category: Miki | [[Category: Miki K]] | ||
[[Category: Nagata | [[Category: Nagata Y]] | ||
[[Category: Peapus | [[Category: Peapus DH]] | ||
Latest revision as of 23:37, 27 December 2023
Fucose-specific lectin from Aleuria aurantia with three ligands
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