3vkm: Difference between revisions
New page: '''Unreleased structure''' The entry 3vkm is ON HOLD Authors: Yoshida, H., Yamashita, S., Teraoka, M., Nakakita, S., Nishi, N., Kamitori, S. Description: Protease-resistant mutant form... |
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==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]] 2.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vkm]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.98Å</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>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:22913484</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vkm" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galectin 3D structures|Galectin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kamitori S]] | |||
[[Category: Nakakita S]] | |||
[[Category: Nishi N]] | |||
[[Category: Teraoka M]] | |||
[[Category: Yamashita S]] | |||
[[Category: Yoshida H]] | |||
Latest revision as of 15:24, 8 November 2023
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
FunctionLEG8_HUMAN Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.[1] Publication Abstract from PubMedGalectin-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 AlsoReferences
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