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| | ==Sugar binding protein - human galectin-2== | | ==Sugar binding protein - human galectin-2== |
| - | <StructureSection load='5dg1' size='340' side='right' caption='[[5dg1]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='5dg1' size='340' side='right'caption='[[5dg1]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dg1]] is a 6 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=5DG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DG1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dg1]] is a 6 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=5DG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DG1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dg2|5dg2]]</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=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS2 ([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=5dg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dg1 OCA], [https://pdbe.org/5dg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dg1 RCSB], [https://www.ebi.ac.uk/pdbsum/5dg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dg1 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dg1 OCA], [http://pdbe.org/5dg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dg1 RCSB], [http://www.ebi.ac.uk/pdbsum/5dg1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dg1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LEG2_HUMAN LEG2_HUMAN]] This protein binds beta-galactoside. Its physiological function is not yet known. | + | [https://www.uniprot.org/uniprot/LEG2_HUMAN LEG2_HUMAN] This protein binds beta-galactoside. Its physiological function is not yet known. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5dg1" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5dg1" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Galectin 3D structures|Galectin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Si, Y L]] | + | [[Category: Large Structures]] |
| - | [[Category: Su, J Y]] | + | [[Category: Si YL]] |
| - | [[Category: Galectin-2]] | + | [[Category: Su JY]] |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
LEG2_HUMAN This protein binds beta-galactoside. Its physiological function is not yet known.
Publication Abstract from PubMed
Galectin-2 (Gal-2) plays a role in cancer, myocardial infarction, immune response, and gastrointestinal tract diseases. The only reported crystal structure of Gal-2 shows that it is a dimer in which the monomer subunits have almost identical structures, each binding with one molecule of lactose. In this study, we crystallized Gal-2 under new conditions that produced three crystal structures. In each Gal-2 dimer structure, lactose was shown to be bound to only one of the carbohydrate recognition domain subunits. In solution studies, the thermal shift assay demonstrated that inequivalent monomer subunits in the Gal-2 dimer become equivalent upon ligand binding. In addition, galectin-mediated erythrocyte agglutination assays using lactose and larger complex polysaccharides as inhibitors showed the structural differences between Gal-1 and Gal-2. Overall, our results reveal some novel aspects to the structural differentiation in Gal-2 and expand the potential for different types of molecular interactions that may be specific to this lectin.
Human galectin-2 interacts with carbohydrates and peptides non-classically: new insight from X-ray crystallography and hemagglutination.,Si Y, Feng S, Gao J, Wang Y, Zhang Z, Meng Y, Zhou Y, Tai G, Su J Acta Biochim Biophys Sin (Shanghai). 2016 Aug 25. PMID:27563008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Si Y, Feng S, Gao J, Wang Y, Zhang Z, Meng Y, Zhou Y, Tai G, Su J. Human galectin-2 interacts with carbohydrates and peptides non-classically: new insight from X-ray crystallography and hemagglutination. Acta Biochim Biophys Sin (Shanghai). 2016 Aug 25. PMID:27563008 doi:http://dx.doi.org/10.1093/abbs/gmw089
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