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5gzc

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<StructureSection load='5gzc' size='340' side='right'caption='[[5gzc]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
<StructureSection load='5gzc' size='340' side='right'caption='[[5gzc]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5gzc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GZC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5gzc]] 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=5GZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GZC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gzd|5gzd]], [[5gze|5gze]], [[5gzf|5gzf]], [[5gzg|5gzg]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gzc OCA], [https://pdbe.org/5gzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gzc RCSB], [https://www.ebi.ac.uk/pdbsum/5gzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gzc ProSAT]</span></td></tr>
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<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=5gzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gzc OCA], [http://pdbe.org/5gzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gzc RCSB], [http://www.ebi.ac.uk/pdbsum/5gzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gzc ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Galectin-8 (Gal-8) plays a significant role in normal immunological function as well as in cancer. This lectin contains two carbohydrate recognition domains (CRD) connected by a peptide linker. The N-terminal CRD determines ligand binding specificity, whereas the linker has been proposed to regulate overall Gal-8 function, including multimerization and biological activity. Here, we crystallized the Gal-8 N-terminal CRD with the peptide linker using a crystallization condition that contains Ni(2+). The Ni(2+) ion was found to be complexed between two CRDs via crystal packing contacts. The coordination between Ni(2+) and Asp25 plays an indirect role in determining the structure of beta-strand F0 and in influencing the linker conformation which could not be defined due to its dynamic nature. The linker was also shortened in situ and crystallized under a different condition, leading to a higher resolution structure refined to 1.08 A. This crystal structure allowed definition of a short portion of the linker interacting with the Gal-8 N-terminal tail via ionic interactions and hydrogen bonds. Observation of two Gal-8 N-terminal CRD structures implies that the N-terminal tail and the linker may influence each other's conformation. In addition, under specific crystallization conditions, glycerol could replace lactose and was observed at the carbohydrate binding site. However, glycerol did not show inhibition activity in hemagglutination assay.
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Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker.,Si Y, Wang Y, Gao J, Song C, Feng S, Zhou Y, Tai G, Su J Int J Mol Sci. 2016 Dec 12;17(12). pii: ijms17122088. doi: 10.3390/ijms17122088. PMID:27973456<ref>PMID:27973456</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5gzc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Si, Y L]]
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[[Category: Si YL]]
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[[Category: Su, J Y]]
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[[Category: Su JY]]
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[[Category: Galectin-8 n-crd structure]]
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[[Category: Sugar binding protein]]
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Current revision

Crystal structure of Galectin-8 N-CRD with part of linker

PDB ID 5gzc

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