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| | <StructureSection load='4xzp' size='340' side='right'caption='[[4xzp]], [[Resolution|resolution]] 1.48Å' scene=''> | | <StructureSection load='4xzp' size='340' side='right'caption='[[4xzp]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xzp]] is a 1 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=4XZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xzp]] is a 1 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=4XZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XZP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cbl|5cbl]]</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=4xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzp OCA], [https://pdbe.org/4xzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xzp RCSB], [https://www.ebi.ac.uk/pdbsum/4xzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzp ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzp OCA], [http://pdbe.org/4xzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xzp RCSB], [http://www.ebi.ac.uk/pdbsum/4xzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzp 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: Nonato, M C]] | + | [[Category: Nonato MC]] |
| - | [[Category: Rustiguel, J K]] | + | [[Category: Rustiguel JK]] |
| - | [[Category: Beta-galactosides binding]]
| + | |
| - | [[Category: Galectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| 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
Galectins are proteins involved in diverse cellular contexts due to their capacity to decipher and respond to the information encoded by beta-galactoside sugars. In particular, human galectin-4, normally expressed in the healthy gastrointestinal tract, displays differential expression in cancerous tissues and is considered a potential drug target for liver and lung cancer. Galectin-4 is a tandem-repeat galectin characterized by two carbohydrate recognition domains connected by a linker-peptide. Despite their relevance to cell function and pathogenesis, structural characterization of full-length tandem-repeat galectins has remained elusive. Here, we investigate galectin-4 using X-ray crystallography, small- and wide-angle X-ray scattering, molecular modelling, molecular dynamics simulations, and differential scanning fluorimetry assays and describe for the first time a structural model for human galectin-4. Our results provide insight into the structural role of the linker-peptide and shed light on the dynamic characteristics of the mechanism of carbohydrate recognition among tandem-repeat galectins.
Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication.,Rustiguel JK, Soares RO, Meisburger SP, Davis KM, Malzbender KL, Ando N, Dias-Baruffi M, Nonato MC Sci Rep. 2016 Sep 19;6:33633. doi: 10.1038/srep33633. PMID:27642006[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rustiguel JK, Soares RO, Meisburger SP, Davis KM, Malzbender KL, Ando N, Dias-Baruffi M, Nonato MC. Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication. Sci Rep. 2016 Sep 19;6:33633. doi: 10.1038/srep33633. PMID:27642006 doi:http://dx.doi.org/10.1038/srep33633
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