1is4
From Proteopedia
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<StructureSection load='1is4' size='340' side='right'caption='[[1is4]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1is4' size='340' side='right'caption='[[1is4]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1is4]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1is4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IS4 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1is4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is4 OCA], [https://pdbe.org/1is4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1is4 RCSB], [https://www.ebi.ac.uk/pdbsum/1is4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1is4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/LEG2_CONMY LEG2_CONMY] This protein binds beta-galactoside. Its physiological function is not yet known. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1is4 ConSurf]. | </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=1is4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45A resolution. The previously determined structure of its isoform, congerin I, had revealed a fold evolution via strand swap; however, the structure of congerin II described here resembles other prototype galectins. A comparison of the two congerin genes with that of several other galectins suggests acceralated evolution of both congerin genes following gene duplication. The presence of a Mes (2-[N-morpholino]ethanesulfonic acid) molecule near the carbohydrate-binding site in the crystal structure points to the possibility of an additional binding site in congerin II. The binding site consists of a group of residues that had been replaced following gene duplication suggesting that the binding site was built under selective pressure. Congerin II may be a protein specialized for biological defense with an affinity for target carbohydrates on parasites' cell surface. | ||
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- | Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication.,Shirai T, Matsui Y, Shionyu-Mitsuyama C, Yamane T, Kamiya H, Ishii C, Ogawa T, Muramoto K J Mol Biol. 2002 Aug 30;321(5):879-89. PMID:12206768<ref>PMID:12206768</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1is4" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Conger myriaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Ishii | + | [[Category: Ishii C]] |
- | [[Category: Kamiya | + | [[Category: Kamiya H]] |
- | [[Category: Matsui | + | [[Category: Matsui Y]] |
- | [[Category: Muramoto | + | [[Category: Muramoto K]] |
- | [[Category: Ogawa | + | [[Category: Ogawa T]] |
- | [[Category: Shionyu-Mitsuyama | + | [[Category: Shionyu-Mitsuyama C]] |
- | [[Category: Shirai | + | [[Category: Shirai T]] |
- | [[Category: Yamane | + | [[Category: Yamane T]] |
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Current revision
LACTOSE-LIGANDED CONGERIN II
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