4ym0: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ym0]] 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=4YM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YM0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ym0]] 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=4YM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YM0 FirstGlance]. <br>
</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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]] 2.3&#8491;</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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=4ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ym0 OCA], [https://pdbe.org/4ym0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ym0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ym0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ym0 ProSAT]</span></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=4ym0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ym0 OCA], [https://pdbe.org/4ym0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ym0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ym0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ym0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[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.
[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;">
== Publication Abstract from PubMed ==
Human galectin-4 is a lectin that is expressed mainly in the gastrointestinal tract and exhibits metastasis-promoting roles in some cancers. Its tandem-repeat nature exhibits two distinct carbohydrate recognition domains allowing cross-linking by simultaneous binding to sulfated and non-sulfated (but not sialylated) glycosphingolipids and glycoproteins; facilitating stabilisation of lipid rafts. Critically, galectin-4 exerts favourable or unfavourable effects depending upon the cancer. Here we report the first X-ray crystallographic structural information on human galectin-4, specifically the C-terminal carbohydrate recognition domain of human (galectin-4C) in complex with lactose, lactose-3'-sulfate, 2'-fucosyllactose, lacto-N-tetraose and lacto-N-neotetraose. These structures enable elucidation of galectin-4C binding fine-specificity towards sulfated and non-sulfated lacto- and neolacto-series sphingolipids as well as to human blood group antigens. Analysis of the lactose-3'-sulfate complex structure shows that galectin-4C does not recognise the sulfate group using any specific amino acid, but binds the ligand nonetheless. Complex structures with lacto-N-tetraose and lacto-N-neotetraose displayed differences in binding interactions exhibited by the non-reducing-end galactose. That of lacto-N-tetraose points outward from the protein surface whereas that of lacto-N-neotetraose interacts directly with the protein. Recognition patterns of human galectin-4C towards lacto- and neolacto-series glycosphingolipids are similar to those of human galectin-3, however detailed scrutiny revealed differences stemming from the extended binding-site that offer distinction in ligand profiles of these two galectins. Structural characterisation of the complex with 2'-fucosyllactose, a carbohydrate with similarity to the H-antigen, and molecular dynamics studies highlight structural features that allow specific recognition of A- and B-antigens, whilst a lack of interaction with the 2'-fucose of blood group antigens was revealed. This article is protected by copyright. All rights reserved.
Structural characterisation of human galectin-4 C-terminal domain -elucidating the molecular basis for recognition of glycosphingolipids, sulfated saccharides and blood group antigens.,Bum-Erdene K, Leffler H, Nilsson UJ, Blanchard H FEBS J. 2015 Jun 16. doi: 10.1111/febs.13348. PMID:26077389<ref>PMID:26077389</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ym0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
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__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 13:03, 1 March 2024

Crystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with lacto-N-tetraose (LNT)

4ym0, resolution 2.30Å

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