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| | <StructureSection load='3vko' size='340' side='right'caption='[[3vko]], [[Resolution|resolution]] 2.08Å' scene=''> | | <StructureSection load='3vko' size='340' side='right'caption='[[3vko]], [[Resolution|resolution]] 2.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vko]] is a 2 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=3VKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VKO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 2.08Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900067:3-sialyl-N-acetyllactosamine'>PRD_900067</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vkl|3vkl]], [[3vkm|3vkm]], [[3vkn|3vkn]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS8 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3vko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vko OCA], [https://pdbe.org/3vko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vko RCSB], [https://www.ebi.ac.uk/pdbsum/3vko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vko 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=3vko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vko OCA], [https://pdbe.org/3vko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vko RCSB], [https://www.ebi.ac.uk/pdbsum/3vko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vko ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN]] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref>
| + | [https://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kamitori, S]] | + | [[Category: Kamitori S]] |
| - | [[Category: Yoshida, H]] | + | [[Category: Yoshida H]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Carbohydrate binding]]
| + | |
| - | [[Category: Oligosaccharide]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
3vko is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.08Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
LEG8_HUMAN Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.[1]
Publication Abstract from PubMed
Galectin-8 is a tandem-repeat-type beta-galactoside-specific animal lectin having N- and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively) with a difference in carbohydrate-binding specificity, involved in cell-matrix interaction, malignant transformation, and cell adhesion. N-CRD exhibits strong affinity for alpha2-3 sialylated oligosaccharides, a feature unique to galectin-8. C-CRD usually exhibits relatively lower affinity for oligosaccharides, but has higher affinity for N-glycan-type branched oligosaccharides than does N-CRD. There have been many structural studies on galectins with a single CRD, but no X-ray structure of a galectin containing both CRDs has been reported. Here, the X-ray structure of a protease-resistant mutant form of human galectin-8 having both CRDs and the novel pseudo-dimer structure of galectin-8 N-CRD in complexes with alpha2-3 sialylated oligosaccharide ligands were determined. The results revealed a difference in specificity between the N- and C-CRDs, and provided new insights into the association of CRDs and/or molecules of galectin-8. (c) 2012 The Authors Journal compilation (c) 2012 FEBS.
X-ray Structure of a Protease-resistant Mutant Form of Human Galectin-8 with Two Carbohydrate Recognition Domains.,Yoshida H, Yamashita S, Teraoka M, Itoh A, Nakakita SI, Nishi N, Kamitori S FEBS J. 2012 Aug 22. doi: 10.1111/j.1742-4658.2012.08753.x. PMID:22913484[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ideo H, Matsuzaka T, Nonaka T, Seko A, Yamashita K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem. 2011 Apr 1;286(13):11346-55. Epub 2011 Feb 2. PMID:21288902 doi:10.1074/jbc.M110.195925
- ↑ Yoshida H, Yamashita S, Teraoka M, Itoh A, Nakakita SI, Nishi N, Kamitori S. X-ray Structure of a Protease-resistant Mutant Form of Human Galectin-8 with Two Carbohydrate Recognition Domains. FEBS J. 2012 Aug 22. doi: 10.1111/j.1742-4658.2012.08753.x. PMID:22913484 doi:10.1111/j.1742-4658.2012.08753.x
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