4agr: Difference between revisions
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[[ | ==Structure of a tetrameric galectin from Cinachyrella sp. (Ball sponge)== | ||
<StructureSection load='4agr' size='340' side='right' caption='[[4agr]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4agr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cinachyrella Cinachyrella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AGR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AGR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4agg|4agg]], [[4agv|4agv]]</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=4agr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4agr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4agr RCSB], [http://www.ebi.ac.uk/pdbsum/4agr PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The galectins are a family of proteins that bind with highest affinity to N-acetyllactosamine disaccharides, which are common constituents of asparagine-linked complex glycans. They play important and diverse physiological roles, particularly in the immune system, and are thought to be critical metastatic agents for many types of cancer cells, including gliomas. A recent bioactivity-based screen of marine sponge (Cinachyrella sp.) extract identified an ancestral member of the galectin family based on its unexpected ability to positively modulate mammalian ionotropic glutamate receptor function. To gain insight into the mechanistic basis of this activity, the 2.1 A resolution X-ray structure of one member of the family, galectin CchG-1, is reported. While the protomer exhibited structural similarity to mammalian prototype galectin, CchG-1 adopts a novel tetrameric arrangement in which a rigid toroidal-shaped `donut' is stabilized in part by the packing of pairs of vicinal disulfide bonds. Twofold symmetry between binding-site pairs provides a basis for a model for interaction with ionotropic glutamate receptors. | |||
Structure of a tetrameric galectin from Cinachyrella sp. (ball sponge).,Freymann DM, Nakamura Y, Focia PJ, Sakai R, Swanson GT Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1163-74. Epub 2012 Aug 18. PMID:22948917<ref>PMID:22948917</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Galectin|Galectin]] | *[[Galectin|Galectin]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cinachyrella]] | [[Category: Cinachyrella]] | ||
[[Category: Focia, P J | [[Category: Focia, P J]] | ||
[[Category: Freymann, D M | [[Category: Freymann, D M]] | ||
[[Category: Sakai, R | [[Category: Sakai, R]] | ||
[[Category: Swanson, G T | [[Category: Swanson, G T]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 20:27, 9 December 2014
Structure of a tetrameric galectin from Cinachyrella sp. (Ball sponge)Structure of a tetrameric galectin from Cinachyrella sp. (Ball sponge)
Structural highlights
Publication Abstract from PubMedThe galectins are a family of proteins that bind with highest affinity to N-acetyllactosamine disaccharides, which are common constituents of asparagine-linked complex glycans. They play important and diverse physiological roles, particularly in the immune system, and are thought to be critical metastatic agents for many types of cancer cells, including gliomas. A recent bioactivity-based screen of marine sponge (Cinachyrella sp.) extract identified an ancestral member of the galectin family based on its unexpected ability to positively modulate mammalian ionotropic glutamate receptor function. To gain insight into the mechanistic basis of this activity, the 2.1 A resolution X-ray structure of one member of the family, galectin CchG-1, is reported. While the protomer exhibited structural similarity to mammalian prototype galectin, CchG-1 adopts a novel tetrameric arrangement in which a rigid toroidal-shaped `donut' is stabilized in part by the packing of pairs of vicinal disulfide bonds. Twofold symmetry between binding-site pairs provides a basis for a model for interaction with ionotropic glutamate receptors. Structure of a tetrameric galectin from Cinachyrella sp. (ball sponge).,Freymann DM, Nakamura Y, Focia PJ, Sakai R, Swanson GT Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1163-74. Epub 2012 Aug 18. PMID:22948917[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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