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==human galectin-16 R55N/H57R== | |||
<StructureSection load='6ljr' size='340' side='right'caption='[[6ljr]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ljr]] 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=6LJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LJR FirstGlance]. <br> | |||
</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=6ljr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljr OCA], [https://pdbe.org/6ljr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ljr RCSB], [https://www.ebi.ac.uk/pdbsum/6ljr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LEG16_HUMAN LEG16_HUMAN] Binds lactose with high affinity. Strong inducer of T-cell apoptosis.<ref>PMID:19497882</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: The structure of human galectin-16 (Gal-16) has yet to be solved, and its function has remained elusive. METHODS: X-ray crystallography was used to determine the atomic structures of Gal-16 and two of its mutants. The Gal-16 oligomer state was investigated by gel filtration, its hemagglutination activity was determined along with its ability to bind lactose using ITC. The cellular distribution of EGFP-tagged Gal-16 in various cell lines was also investigated, and the interaction between Gal-16 and c-Rel was assessed by pull-down studies, microscale thermophoresis and immunofluorescence. RESULTS: Unlike other galectins, Gal-16 lacks the ability to bind the beta-galactoside lactose. Lactose binding could be regained by replacing an arginine (Arg55) with asparagine, as shown in the crystal structures of two lactose-loaded Gal-16 mutants (R55N and R55N/H57R). Gal-16 was also shown to be monomeric by gel filtration, as well as in crystal structures. Thus, this galectin could not induce erythrocyte agglutination. EGFP-tagged Gal-16 was found to be localized mostly in the nucleus of various cell types, and can interact with c-Rel, a member of NF-kappaB family. CONCLUSIONS: Gal-16 exists as a monomer and its ligand binding is significantly different from that of other prototype galectins, suggesting that it has a novel function(s). The interaction between Gal-16 and c-Rel indicates that Gal-16 may regulate signal transduction pathways via the c-Rel hub in B or T cells at the maternal-fetal interface. GENERAL SIGNIFICANCE: The present study lays the foundation for further studies into the cellular and physiological functions of Gal-16. | |||
Human galectin-16 has a pseudo ligand binding site and plays a role in regulating c-Rel-mediated lymphocyte activity.,Si Y, Yao Y, Jaramillo Ayala G, Li X, Han Q, Zhang W, Xu X, Tai G, Mayo KH, Zhou Y, Su J Biochim Biophys Acta Gen Subj. 2020 Oct 2;1865(1):129755. doi:, 10.1016/j.bbagen.2020.129755. PMID:33011338<ref>PMID:33011338</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Su | <div class="pdbe-citations 6ljr" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Su J]] | |||
Latest revision as of 14:02, 22 November 2023
human galectin-16 R55N/H57Rhuman galectin-16 R55N/H57R
Structural highlights
FunctionLEG16_HUMAN Binds lactose with high affinity. Strong inducer of T-cell apoptosis.[1] Publication Abstract from PubMedBACKGROUND: The structure of human galectin-16 (Gal-16) has yet to be solved, and its function has remained elusive. METHODS: X-ray crystallography was used to determine the atomic structures of Gal-16 and two of its mutants. The Gal-16 oligomer state was investigated by gel filtration, its hemagglutination activity was determined along with its ability to bind lactose using ITC. The cellular distribution of EGFP-tagged Gal-16 in various cell lines was also investigated, and the interaction between Gal-16 and c-Rel was assessed by pull-down studies, microscale thermophoresis and immunofluorescence. RESULTS: Unlike other galectins, Gal-16 lacks the ability to bind the beta-galactoside lactose. Lactose binding could be regained by replacing an arginine (Arg55) with asparagine, as shown in the crystal structures of two lactose-loaded Gal-16 mutants (R55N and R55N/H57R). Gal-16 was also shown to be monomeric by gel filtration, as well as in crystal structures. Thus, this galectin could not induce erythrocyte agglutination. EGFP-tagged Gal-16 was found to be localized mostly in the nucleus of various cell types, and can interact with c-Rel, a member of NF-kappaB family. CONCLUSIONS: Gal-16 exists as a monomer and its ligand binding is significantly different from that of other prototype galectins, suggesting that it has a novel function(s). The interaction between Gal-16 and c-Rel indicates that Gal-16 may regulate signal transduction pathways via the c-Rel hub in B or T cells at the maternal-fetal interface. GENERAL SIGNIFICANCE: The present study lays the foundation for further studies into the cellular and physiological functions of Gal-16. Human galectin-16 has a pseudo ligand binding site and plays a role in regulating c-Rel-mediated lymphocyte activity.,Si Y, Yao Y, Jaramillo Ayala G, Li X, Han Q, Zhang W, Xu X, Tai G, Mayo KH, Zhou Y, Su J Biochim Biophys Acta Gen Subj. 2020 Oct 2;1865(1):129755. doi:, 10.1016/j.bbagen.2020.129755. PMID:33011338[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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