3vkm: Difference between revisions

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==Protease-resistant mutant form of Human Galectin-8 in complex with sialyllactose and lactose==
==Protease-resistant mutant form of Human Galectin-8 in complex with sialyllactose and lactose==
<StructureSection load='3vkm' size='340' side='right' caption='[[3vkm]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
<StructureSection load='3vkm' size='340' side='right'caption='[[3vkm]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vkm]] is a 2 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=3VKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VKM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3vkm]] 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=3VKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VKM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fqz|4fqz]], [[3vkl|3vkl]], [[3vkn|3vkn]], [[3vko|3vko]]</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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4fqz|4fqz]], [[3vkl|3vkl]], [[3vkn|3vkn]], [[3vko|3vko]]</div></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=3vkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkm OCA], [http://pdbe.org/3vkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vkm RCSB], [http://www.ebi.ac.uk/pdbsum/3vkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vkm ProSAT]</span></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=3vkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkm OCA], [https://pdbe.org/3vkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vkm RCSB], [https://www.ebi.ac.uk/pdbsum/3vkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vkm 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>   
[[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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</div>
</div>
<div class="pdbe-citations 3vkm" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3vkm" style="background-color:#fffaf0;"></div>
==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Kamitori, S]]
[[Category: Kamitori, S]]
[[Category: Nakakita, S]]
[[Category: Nakakita, S]]

Revision as of 21:50, 27 July 2022

Protease-resistant mutant form of Human Galectin-8 in complex with sialyllactose and lactoseProtease-resistant mutant form of Human Galectin-8 in complex with sialyllactose and lactose

Structural highlights

3vkm is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
NonStd Res:
Gene:LGALS8 (HUMAN)
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

  1. 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
  2. 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

3vkm, resolution 2.98Å

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