View source for 4agv


==Structure of a tetrameric galectin from Cinachyrella sp. (Ball sponge)==
<StructureSection load='4agv' size='340' side='right'caption='[[4agv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4agv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cinachyrella Cinachyrella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AGV 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]] 2.65&#8491;</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=4agv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4agv OCA], [https://pdbe.org/4agv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4agv RCSB], [https://www.ebi.ac.uk/pdbsum/4agv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4agv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I0IV54_9METZ I0IV54_9METZ] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4agv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cinachyrella]]
[[Category: Large Structures]]
[[Category: Focia PJ]]
[[Category: Freymann DM]]
[[Category: Sakai R]]
[[Category: Swanson GT]]