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| | ==Galectin-13/Placental Protein 13 crystal structure== | | ==Galectin-13/Placental Protein 13 crystal structure== |
| - | <StructureSection load='5xg7' size='340' side='right' caption='[[5xg7]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='5xg7' size='340' side='right'caption='[[5xg7]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xg7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XG7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xg7]] 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=5XG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XG7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xg8|5xg8]]</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]] 1.55Å</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=5xg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xg7 OCA], [http://pdbe.org/5xg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xg7 RCSB], [http://www.ebi.ac.uk/pdbsum/5xg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xg7 ProSAT]</span></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=5xg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xg7 OCA], [https://pdbe.org/5xg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xg7 RCSB], [https://www.ebi.ac.uk/pdbsum/5xg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xg7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PP13_HUMAN PP13_HUMAN]] Binds beta-galactoside and lactose. Strong inducer of T-cell apoptosis.<ref>PMID:10527825</ref> <ref>PMID:19497882</ref> | + | [https://www.uniprot.org/uniprot/PP13_HUMAN PP13_HUMAN] Binds beta-galactoside and lactose. Strong inducer of T-cell apoptosis.<ref>PMID:10527825</ref> <ref>PMID:19497882</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | During pregnancy, placental protein-13 (galectin-13) is highly expressed in the placenta and fetal tissue, and less so in maternal serum that is related to pre-eclampsia. To understand galectin-13 function at the molecular level, we solved its crystal structure and discovered that its dimer is stabilized by two disulfide bridges between Cys136 and Cys138 and six hydrogen bonds involving Val135, Val137, and Gln139. Native PAGE and gel filtration demonstrate that this is not a crystallization artifact because dimers also form in solution. Our biochemical studies indicate that galectin-13 ligand binding specificity is different from that of other galectins in that it does not bind beta-galactosides. This is partly explained by the presence of Arg53 rather than His53 at the bottom of the carbohydrate binding site in a position that is crucial for interactions with beta-galactosides. Mutating Arg53 to histidine does not re-establish normal beta-galactoside binding, but rather traps cryoprotectant glycerol molecules within the ligand binding site in crystals of the R53H mutant. Moreover, unlike most other galectins, we also found that GFP-tagged galectin-13 is localized within the nucleus of HeLa and 293 T cells. Overall, galectin-13 appears to be a new type of prototype galectin with distinct properties.
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| - | Galectin-13, a different prototype galectin, does not bind beta-galacto-sides and forms dimers via intermolecular disulfide bridges between Cys-136 and Cys-138.,Su J, Wang Y, Si Y, Gao J, Song C, Cui L, Wu R, Tai G, Zhou Y Sci Rep. 2018 Jan 17;8(1):980. doi: 10.1038/s41598-018-19465-0. PMID:29343868<ref>PMID:29343868</ref>
| + | ==See Also== |
| - | | + | *[[Galectin 3D structures|Galectin 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5xg7" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Su, J Y]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Wang, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Galectin-13/placental protein 13 crystal structure]] | + | [[Category: Su JY]] |
| - | [[Category: Sugar binding protein]] | + | [[Category: Wang Y]] |
| Structural highlights
Function
PP13_HUMAN Binds beta-galactoside and lactose. Strong inducer of T-cell apoptosis.[1] [2]
See Also
References
- ↑ Than NG, Sumegi B, Than GN, Berente Z, Bohn H. Isolation and sequence analysis of a cDNA encoding human placental tissue protein 13 (PP13), a new lysophospholipase, homologue of human eosinophil Charcot-Leyden Crystal protein. Placenta. 1999 Nov;20(8):703-10. PMID:10527825 doi:http://dx.doi.org/10.1053/plac.1999.0436
- ↑ Than NG, Romero R, Goodman M, Weckle A, Xing J, Dong Z, Xu Y, Tarquini F, Szilagyi A, Gal P, Hou Z, Tarca AL, Kim CJ, Kim JS, Haidarian S, Uddin M, Bohn H, Benirschke K, Santolaya-Forgas J, Grossman LI, Erez O, Hassan SS, Zavodszky P, Papp Z, Wildman DE. A primate subfamily of galectins expressed at the maternal-fetal interface that promote immune cell death. Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9731-6. doi:, 10.1073/pnas.0903568106. Epub 2009 Jun 2. PMID:19497882 doi:http://dx.doi.org/10.1073/pnas.0903568106
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