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4rl7
From Proteopedia
(Difference between revisions)
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==Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.5, PEG6000)== | ==Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.5, PEG6000)== | ||
| - | <StructureSection load='4rl7' size='340' side='right'caption='[[4rl7]]' scene=''> | + | <StructureSection load='4rl7' size='340' side='right'caption='[[4rl7]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rl7]] 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=4RL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RL7 FirstGlance]. <br> |
| - | </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=4rl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rl7 OCA], [https://pdbe.org/4rl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rl7 RCSB], [https://www.ebi.ac.uk/pdbsum/4rl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rl7 ProSAT]</span></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]] 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=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'>[https://proteopedia.org/fgij/fg.htm?mol=4rl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rl7 OCA], [https://pdbe.org/4rl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rl7 RCSB], [https://www.ebi.ac.uk/pdbsum/4rl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rl7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LEG3_HUMAN 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.<ref>PMID:15181153</ref> <ref>PMID:19594635</ref> <ref>PMID:19616076</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Galectin-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<ref>PMID:25662390</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4rl7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Galectin 3D structures|Galectin 3D structures]] | *[[Galectin 3D structures|Galectin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Su JY]] | [[Category: Su JY]] | ||
Current revision
Crystal structure of Human galectin-3 CRD in complex with lactose (pH 7.5, PEG6000)
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