1is5

<StructureSection load='1is5' size='340' side='right' caption='[[1is5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1is5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IS5 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c1f|1c1f]], [[1is3|1is3]], [[1is4|1is4]], [[1is6|1is6]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1is5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is5 OCA], [http://pdbe.org/1is5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1is5 RCSB], [http://www.ebi.ac.uk/pdbsum/1is5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1is5 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/LEG2_CONMY LEG2_CONMY]] This protein binds beta-galactoside. Its physiological function is not yet known.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/1is5_consurf.spt"</scriptWhenChecked>

<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/>

[[Category: Anguilla myriaster]]

[[Category: Ishii, C]]

[[Category: Kamiya, H]]

[[Category: Matsui, Y]]

[[Category: Muramoto, K]]

[[Category: Ogawa, T]]

[[Category: Shionyu-Mitsuyama, C]]

[[Category: Shirai, T]]

[[Category: Yamane, T]]

[[Category: Sugar binding protein]]