3wuc

<StructureSection load='3wuc' size='340' side='right'caption='[[3wuc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[3wuc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUC FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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=3wuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wuc OCA], [https://pdbe.org/3wuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wuc RCSB], [https://www.ebi.ac.uk/pdbsum/3wuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wuc ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Xenopus laevis (African clawed frog) has two types of proto-type galectins that are similar to mammalian galectin-1 in amino acid sequence. One type, comprising xgalectin-Ia and -Ib, is regarded as being equivalent to galectin-1, and the other type, comprising xgalectin-Va and -Vb, is expected to be a unique galectin subgroup. The latter is considerably abundant in frog skin, however, its biological function remains unclear. We determined the crystal structures of two proto-type galectins, xgalectin-Ib and -Va. The structures showed that both galectins formed a mammalian galectin-1-like homodimer, and furthermore, xgalectin-Va formed a homotetramer. This tetramer structure has not been reported for other galectins. Gel filtration and other experiments indicated that xgalectin-Va was in a dimer-tetramer equilibrium in solution, and lactose binding enhanced the tetramer formation. The residues involved in the dimer-dimer association were conserved in xgalectin-Va and -Vb, and one of the Xenopus (Silurana) tropicalis proto-type galectins, but not in xgalectin-Ia and -Ib, and other galectin-1-equivalent proteins. Xgalectin-Va preferred Galbeta1-3GalNAc and not Galbeta1-4GlcNAc, while xgalectin-Ib preferred Galbeta1-4GlcNAc as well as human galectin-1. Xgalectin-Va/Vb would have diverged from the galectin-1 group with accompanying acquisition of the higher oligomer formation and altered ligand selectivity.

Crystal structure of a Xenopus laevis skin proto-type galectin, close to but distinct from galectin-1.,Nonaka Y, Ogawa T, Yoshida H, Shoji H, Nishi N, Kamitori S, Nakamura T Glycobiology. 2015 Mar 24. pii: cwv020. PMID:25804418<ref>PMID:25804418</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3wuc" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Kamitori, S]]

[[Category: Nakamura, T]]

[[Category: Nonaka, Y]]

[[Category: Yoshida, H]]

[[Category: Sugar binding protein]]