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| | <StructureSection load='5duw' size='340' side='right'caption='[[5duw]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5duw' size='340' side='right'caption='[[5duw]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5duw]] 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=5DUW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DUW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5duw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DUW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GO:4-O-(3-O-SULFO-BETA-D-GALACTOPYRANOSYL)-BETA-D-GLUCOPYRANOSE'>5GO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5duu|5duu]], [[5duv|5duv]], [[5dux|5dux]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900068:lactose-3-sulfate'>PRD_900068</scene>, <scene name='pdbligand=SGA:O3-SULFONYLGALACTOSE'>SGA</scene></td></tr> |
| - | <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'>[https://proteopedia.org/fgij/fg.htm?mol=5duw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5duw OCA], [https://pdbe.org/5duw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5duw RCSB], [https://www.ebi.ac.uk/pdbsum/5duw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5duw ProSAT]</span></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=5duw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5duw OCA], [http://pdbe.org/5duw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5duw RCSB], [http://www.ebi.ac.uk/pdbsum/5duw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5duw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LEG4_HUMAN LEG4_HUMAN]] Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. | + | [https://www.uniprot.org/uniprot/LEG4_HUMAN LEG4_HUMAN] Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blanchard, H]] | + | [[Category: Blanchard H]] |
| - | [[Category: Bum-Erdene, K]] | + | [[Category: Bum-Erdene K]] |
| - | [[Category: Galectin-4]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| - | [[Category: Sugar-binding protein]]
| + | |
| - | [[Category: Sulfate]]
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| 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 PubMed
Galectin-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 Also
References
- ↑ Bum-Erdene K, Leffler H, Nilsson UJ, Blanchard H. Structural characterisation of human galectin-4 N-terminal carbohydrate recognition domain in complex with glycerol, lactose, 3'-sulfo-lactose, and 2'-fucosyllactose. Sci Rep. 2016 Feb 1;6:20289. doi: 10.1038/srep20289. PMID:26828567 doi:http://dx.doi.org/10.1038/srep20289
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