5duv: Difference between revisions
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==Crystal structure of the human galectin-4 N-terminal carbohydrate recognition domain in complex with lactose== | ==Crystal structure of the human galectin-4 N-terminal carbohydrate recognition domain in complex with lactose== | ||
<StructureSection load='5duv' size='340' side='right' caption='[[5duv]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5duv' size='340' side='right'caption='[[5duv]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5duv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUV OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5duv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DUV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5duu|5duu]], [[5duw|5duw]], [[5dux|5dux]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5duu|5duu]], [[5duw|5duw]], [[5dux|5dux]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5duv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5duv OCA], [http://pdbe.org/5duv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5duv RCSB], [http://www.ebi.ac.uk/pdbsum/5duv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5duv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5duv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5duv" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Blanchard, H]] | [[Category: Blanchard, H]] | ||
[[Category: Bum-Erdene, K]] | [[Category: Bum-Erdene, K]] | ||
Revision as of 11:07, 15 April 2020
Crystal structure of the human galectin-4 N-terminal carbohydrate recognition domain in complex with lactoseCrystal structure of the human galectin-4 N-terminal carbohydrate recognition domain in complex with lactose
Structural highlights
Function[LEG4_HUMAN] Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. Publication Abstract from PubMedGalectin-4 is a tandem-repeat galectin with two distinct carbohydrate recognition domains (CRD). Galectin-4 is expressed mainly in the alimentary tract and is proposed to function as a lipid raft and adherens junction stabilizer by its glycan cross-linking capacity. Galectin-4 plays divergent roles in cancer and inflammatory conditions, either promoting or inhibiting each disease progression, depending on the specific pathological condition. The study of galectin-4's ligand-binding profile may help decipher its roles under specific conditions. Here we present the X-ray structures of human galectin-4 N-terminal CRD (galectin-4N) bound to different saccharide ligands. Galectin-4's overall fold and its core interactions to lactose are similar to other galectin CRDs. Galectin-4N recognises the sulfate cap of 3'-sulfated glycans by a weak interaction through Arg45 and two water-mediated hydrogen bonds via Trp84 and Asn49. When galectin-4N interacts with the H-antigen mimic, 2'-fucosyllactose, an interaction is formed between the ring oxygen of fucose and Arg45. The extended binding site of galectin-4N may not be well suited to the A/B-antigen determinants, alpha-GalNAc/alpha-Gal, specifically due to clashes with residue Phe47. Overall, galectin-4N favours sulfated glycans whilst galectin-4C prefers blood group determinants. However, the two CRDs of galectin-4 can, to a less extent, recognise each other's ligands. Structural characterisation of human galectin-4 N-terminal carbohydrate recognition domain in complex with glycerol, lactose, 3'-sulfo-lactose, and 2'-fucosyllactose.,Bum-Erdene K, Leffler H, Nilsson UJ, Blanchard H Sci Rep. 2016 Feb 1;6:20289. doi: 10.1038/srep20289. PMID:26828567[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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