View source for 4wvv


==Chicken Galectin-8 N-terminal domain complexed with lactose==
<StructureSection load='4wvv' size='340' side='right'caption='[[4wvv]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wvv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WVV 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]] 1.205&#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></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=4wvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvv OCA], [https://pdbe.org/4wvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wvv RCSB], [https://www.ebi.ac.uk/pdbsum/4wvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1W2P6_CHICK Q1W2P6_CHICK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The physiological significance arising from translating information stored in glycans into cellular effects explains the interest in structurally defining lectin-carbohydrate recognition. The relatively small set of adhesion/growth-regulatory galectins in chicken makes this system attractive to study the origins of specificity and divergence. Cell binding by using glycosylation mutants reveals binding of the N-terminal domain of chicken galectin-8 (CG-8N) to alpha-2,3-sialylated and galactose-terminated glycan chains. Cocrystals with lactose and its 3'-sialylated derivative disclose Arg58 as a key contact for the carboxylic acid and differences in loop lengths to the three homodimeric chicken galectins. Monitoring hydrogen-deuterium exchange by mass spectrometry revealed an effective reduction of deuteration after ligand binding within the contact area. In addition, evidence for changes in solvent accessibility of amide protons beyond this site was obtained. Their detection, which highlights the sensor capacity of this technique, encourages systematic studies on galectins and beyond.

Combining Crystallography and Hydrogen-Deuterium Exchange to Study Galectin-Ligand Complexes.,Ruiz FM, Gilles U, Lindner I, Andre S, Romero A, Reusch D, Gabius HJ Chemistry. 2015 Sep 21;21(39):13558-68. doi: 10.1002/chem.201501961. Epub 2015, Aug 13. PMID:26270612<ref>PMID:26270612</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wvv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Romero A]]
[[Category: Ruiz FM]]