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7rdp

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Revision as of 05:26, 8 September 2022

Crystal structure of human galectin-3 CRD in complex with selenodigalactoside

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7rdp"

Categories: Homo sapiens | Large Structures | Blanchard H | Go RM | Kishor C

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 <StructureSection load='7rdp' size='340' side='right'caption='[[7rdp]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7rdp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RDP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7rdp]] 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=7RDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RDP FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IZ:beta-D-galactopyranosyl+1-seleno-beta-D-galactopyranoside'>4IZ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7rdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rdp OCA], [https://pdbe.org/7rdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rdp RCSB], [https://www.ebi.ac.uk/pdbsum/7rdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rdp ProSAT]</span></td></tr>
 </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 ==
-Human galectin-3 (hGal-3) is involved in a variety of biological processes and is implicated in wide range of diseases. As a result, targeting hGal-3 for clinical applications has become an intense area of research. As a step towards the development of novel hGal-3 inhibitors, we describe a study of the binding of two Se-containing hGal-3 inhibitors, specifically that of di(beta-D-galactopyranosyl)selenide (SeDG), in which two galactose rings are linked by one Se atom and a di(beta-D-galactopyranosyl)diselenide (DSeDG) analogue with a diseleno bond between the two sugar units. The binding affinities of these derivatives to hGal-3 were determined by (15)N-(1)H HSQC NMR spectroscopy and fluorescence anisotropy titrations in solution, indicating a slight decrease in the strength of interaction for SeDG compared to thiodigalactoside (TDG), a well-known inhibitor of hGal-3, while DSeDG displayed a much weaker interaction strength. NMR and FA measurements showed that both seleno derivatives bind to the canonical S face site of hGal-3 and stack against the conserved W181 residue also confirmed by X-ray crystallography, revealing canonical properties of the interaction. The interaction with DSeDG revealed two distinct binding modes in the crystal structure which are in fast exchange on the NMR time scale in solution, explaining a weaker interaction with hGal-3 than SeDG. Using molecular dynamics simulations, we have found that energetic contributions to the binding enthalpies mainly differ in the electrostatic interactions and in polar solvation terms and are responsible for weaker binding of DSeDG compared to SeDG. Selenium-containing carbohydrate inhibitors of hGal-3 showing canonical binding modes offer the potential of becoming novel hydrolytically stable scaffolds for a new class of hGal-3 inhibitors.
-Investigation of the Molecular Details of the Interactions of Selenoglycosides and Human Galectin-3.,Raics M, Balogh AK, Kishor C, Timari I, Medrano FJ, Romero A, Go RM, Blanchard H, Szilagyi L, E Kover K, Feher K Int J Mol Sci. 2022 Feb 24;23(5). pii: ijms23052494. doi: 10.3390/ijms23052494. PMID:35269646<ref>PMID:35269646</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7rdp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Blanchard, H]]
+[[Category: Blanchard H]]
-[[Category: Go, R M]]
+[[Category: Go RM]]
-[[Category: Kishor, C]]
+[[Category: Kishor C]]
-[[Category: Carbohydrate-binding protein]]
-[[Category: Galectin]]
-[[Category: Sugar binding protein]]

7rdp

From Proteopedia

Revision as of 05:26, 8 September 2022

Crystal structure of human galectin-3 CRD in complex with selenodigalactoside

Structural highlights

Function

References

Contents

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