4ym1: Difference between revisions
New page: '''Unreleased structure''' The entry 4ym1 is ON HOLD Authors: Bum-Erdene, K., Blanchard, H. Description: Category: Unreleased Structures Category: Blanchard, H [[Category: Bum... |
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==Crystal structure of the human galectin-4 C-terminal carbohydrate recognition domain in complex with 2'-fucosyllactose== | |||
<StructureSection load='4ym1' size='340' side='right'caption='[[4ym1]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ym1]] 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=4YM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YM1 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]] 2Å</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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900070:2-fucosyllactose'>PRD_900070</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ym1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ym1 OCA], [https://pdbe.org/4ym1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ym1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ym1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ym1 ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Blanchard | <div class="pdbe-citations 4ym1" style="background-color:#fffaf0;"></div> | ||
[[Category: Bum-Erdene | |||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Blanchard H]] | |||
[[Category: Bum-Erdene K]] | |||