3aye: Difference between revisions

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-[[Image:3aye.png|left|200px]]
-{{STRUCTURE_3aye|  PDB=3aye  |  SCENE=  }}
+==Crystal structure of galectin-3 CRD domian complexed with lactose==
+<StructureSection load='3aye' size='340' side='right'caption='[[3aye]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3aye]] 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=3AYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AYE 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&#8491;</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3aye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aye OCA], [https://pdbe.org/3aye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aye RCSB], [https://www.ebi.ac.uk/pdbsum/3aye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aye ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LEG3_HUMAN LEG3_HUMAN] Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells.<ref>PMID:15181153</ref> <ref>PMID:19594635</ref> <ref>PMID:19616076</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Thomsen-Friedenreich (TF or T) antigen, Galbeta1-3GalNAcalpha1-O-Ser/Thr, is the core 1 structure of O-linked mucin type glycans appearing in tumor-associated glycosylation. The TF antigen occurs in about 90% of human cancer cells and is a potential ligand for the human endogenous galectins. It has been reported that human galectin-1 (Gal-1) and galectin-3 (Gal-3) can perform their cancer-related functions via specifically recognizing TF antigen. However, the detailed binding properties have not been clarified and structurally characterized. In this work, first we identified the distinct TF-binding abilities of Gal-1 and Gal-3. The affinity to TF antigen for Gal-3 is two orders of magnitude higher than that for Gal-1. The structures of Gal-3 carbohydrate recognition domain (CRD) complexed with TF antigen and derivatives, TFN and GM1, were then determined. These structures show a unique Glu-water-Arg-water motif-based mode as previously observed in the mushroom galectin AAL. The observation demonstrates that this recognition mode is commonly adopted by TF-binding galectins, either as endogenous or exogenous ones. The detailed structural comparisons between Gal-1 and Gal-3 CRD and mutagenesis experiments reveal that a pentad residue motif ((51)AHGDA(55)) at the loop (g1-L4) connecting beta-strands 4 and 5 of Gal-1 produces a serious steric hindrance for TF binding. This motif is the main structural basis for Gal-1 with the low affinity to TF antigen. These findings provide the intrinsic structural elements for regulating the TF-binding activity of Gal-1 in some special conditions and also show certain target and approach for mediating some tumor-related bioactivities of human galectins.
-===Crystal structure of galectin-3 CRD domian complexed with lactose===
+Structural basis for distinct binding properties of the human galectins to thomsen-friedenreich antigen.,Bian CF, Zhang Y, Sun H, Li DF, Wang DC PLoS One. 2011;6(9):e25007. Epub 2011 Sep 20. PMID:21949831<ref>PMID:21949831</ref>
-{{ABSTRACT_PUBMED_21949831}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3aye" style="background-color:#fffaf0;"></div>
-[[3aye]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AYE OCA].
 ==See Also==
-*[[Galectin|Galectin]]
+*[[Galectin 3D structures|Galectin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021949831</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bian, C F.]]
+[[Category: Large Structures]]
-[[Category: Li, D F.]]
+[[Category: Bian CF]]
-[[Category: Wang, D C.]]
+[[Category: Li DF]]
-[[Category: A -galactose-binding protein]]
+[[Category: Wang DC]]
-[[Category: Beta-galactoside]]
-[[Category: Cell-surface]]
-[[Category: Nuclear]]
-[[Category: Rossmann fold]]
-[[Category: Sugar binding protein]]