1is5: Difference between revisions

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<StructureSection load='1is5' size='340' side='right'caption='[[1is5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1is5' size='340' side='right'caption='[[1is5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1is5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anguilla_myriaster Anguilla myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IS5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1is5]] 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=1IS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IS5 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c1f|1c1f]], [[1is3|1is3]], [[1is4|1is4]], [[1is6|1is6]]</div></td></tr>
</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&#8491;</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=1is5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is5 OCA], [https://pdbe.org/1is5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1is5 RCSB], [https://www.ebi.ac.uk/pdbsum/1is5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1is5 ProSAT]</span></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=1is5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is5 OCA], [https://pdbe.org/1is5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1is5 RCSB], [https://www.ebi.ac.uk/pdbsum/1is5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1is5 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.  
[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=1is5 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=1is5 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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1is5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anguilla myriaster]]
[[Category: Conger myriaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ishii, C]]
[[Category: Ishii C]]
[[Category: Kamiya, H]]
[[Category: Kamiya H]]
[[Category: Matsui, Y]]
[[Category: Matsui Y]]
[[Category: Muramoto, K]]
[[Category: Muramoto K]]
[[Category: Ogawa, T]]
[[Category: Ogawa T]]
[[Category: Shionyu-Mitsuyama, C]]
[[Category: Shionyu-Mitsuyama C]]
[[Category: Shirai, T]]
[[Category: Shirai T]]
[[Category: Yamane, T]]
[[Category: Yamane T]]
[[Category: Beta sandwich]]
[[Category: Sugar binding protein]]

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