View source for 3wud


==X-ray crystal structure of Xenopus laevis galectin-Ib==
<StructureSection load='3wud' size='340' side='right'caption='[[3wud]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUD 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]] 1.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</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=3wud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wud OCA], [https://pdbe.org/3wud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wud RCSB], [https://www.ebi.ac.uk/pdbsum/3wud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wud ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q98UD4_XENLA Q98UD4_XENLA] 
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 3wud" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Kamitori S]]
[[Category: Nakamura T]]
[[Category: Nonaka Y]]
[[Category: Yoshida H]]