5gzd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Galectin-8 N-terminal domain carbohydrate recognition domain== | ==Galectin-8 N-terminal domain carbohydrate recognition domain== | ||
<StructureSection load='5gzd' size='340' side='right' caption='[[5gzd]], [[Resolution|resolution]] 1.19Å' scene=''> | <StructureSection load='5gzd' size='340' side='right'caption='[[5gzd]], [[Resolution|resolution]] 1.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gzd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GZD FirstGlance]. <br> | <table><tr><td colspan='2'>[[5gzd]] 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=5GZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GZD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gzc|5gzc]], [[5gze|5gze]], [[5gzf|5gzf]], [[5gzg|5gzg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gzc|5gzc]], [[5gze|5gze]], [[5gzf|5gzf]], [[5gzg|5gzg]]</td></tr> | ||
<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> | |||
<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=5gzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gzd OCA], [http://pdbe.org/5gzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gzd RCSB], [http://www.ebi.ac.uk/pdbsum/5gzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gzd ProSAT]</span></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=5gzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gzd OCA], [http://pdbe.org/5gzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gzd RCSB], [http://www.ebi.ac.uk/pdbsum/5gzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gzd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[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> | [[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> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5gzd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Si, Y L]] | [[Category: Si, Y L]] | ||
[[Category: Su, J Y]] | [[Category: Su, J Y]] | ||
[[Category: Galectin-8 n-terminal domain carbohydrate recognition domain]] | [[Category: Galectin-8 n-terminal domain carbohydrate recognition domain]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||