4ym3: Difference between revisions
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==Crystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with lactose== | ==Crystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with lactose== | ||
<StructureSection load='4ym3' size='340' side='right' caption='[[4ym3]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='4ym3' size='340' side='right'caption='[[4ym3]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ym3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YM3 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4ym3]] 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=4YM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YM3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> | ||
<tr id=' | <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=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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ym3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ym3 OCA], [https://pdbe.org/4ym3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ym3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ym3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ym3 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ym3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Blanchard H]] | ||
[[Category: | [[Category: Bum-Erdene K]] | ||
Latest revision as of 11:02, 27 September 2023
Crystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with lactoseCrystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with lactose
Structural highlights
FunctionLEG4_HUMAN Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. Publication Abstract from PubMedHuman 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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