4r9a: Difference between revisions
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==Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.0, PEG4000)== | ==Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.0, PEG4000)== | ||
<StructureSection load='4r9a' size='340' side='right' caption='[[4r9a]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='4r9a' size='340' side='right'caption='[[4r9a]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4r9a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R9A FirstGlance]. <br> | <table><tr><td colspan='2'>[[4r9a]] 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=4R9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R9A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r9b|4r9b]], [[4r9c|4r9c]], [[4r9d|4r9d]], [[4rl7|4rl7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r9b|4r9b]], [[4r9c|4r9c]], [[4r9d|4r9d]], [[4rl7|4rl7]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS3, MAC2 ([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=4r9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9a OCA], [http://pdbe.org/4r9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r9a RCSB], [http://www.ebi.ac.uk/pdbsum/4r9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9a 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=4r9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9a OCA], [http://pdbe.org/4r9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r9a RCSB], [http://www.ebi.ac.uk/pdbsum/4r9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Su, J Y]] | [[Category: Su, J Y]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 13:12, 1 May 2019
Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.0, PEG4000)Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.0, PEG4000)
Structural highlights
Function[LEG3_HUMAN] Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells.[1] [2] [3] Publication Abstract from PubMedGalectin-3 (Gal-3) which shows affinity of beta-galactosides is a cancer-related protein. Thus, it is important to understand its ligand binding mechanism and then design its specific inhibitor. It was suggested that the positions of water molecules in Gal-3 ligand-binding site could be replaced by appropriate chemical groups of ideal inhibitors. However, the reported structures of Gal-3 carbohydrate recognition domain (CRD) complexed with lactose showed that the number of water molecules are different and the water positions are inconsistent in the ligand-binding site. This study reported four high-resolution (1.24-1.19 A) structures of Gal-3 CRD complexed with lactose, and accurately located 12 conserved water molecules in the water network of Gal-3 CRD ligand-binding site by merging these structures. These water molecules either directly stabilize the binding of Gal-3 CRD and lactose, or hold the former water molecules at the right place. In particular, water molecule 4 (W4) which only coordinates with water molecule 5 (W5) and water molecule 6 (W6) plays a key role in stabilizing galactose residue. In addition, by three-dimensional alignment of the positions of all residues, 14 flexible parts of Gal-3 CRD were found to dynamically fluctuate in the crystalline environment. The water network in galectin-3 ligand binding site guides inhibitor design.,Su J, Zhang T, Wang P, Liu F, Tai G, Zhou Y Acta Biochim Biophys Sin (Shanghai). 2015 Mar;47(3):192-8. doi:, 10.1093/abbs/gmu132. Epub 2015 Feb 5. PMID:25662390[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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