4xzp: Difference between revisions

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 ==Crystal structure of the N-terminal domain of human galectin-4==
-<StructureSection load='4xzp' size='340' side='right' caption='[[4xzp]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
+<StructureSection load='4xzp' size='340' side='right'caption='[[4xzp]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xzp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xzp]] is a 1 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=4XZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XZP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cbl|5cbl]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzp OCA], [http://pdbe.org/4xzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xzp RCSB], [http://www.ebi.ac.uk/pdbsum/4xzp PDBsum]</span></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=4xzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzp OCA], [https://pdbe.org/4xzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xzp RCSB], [https://www.ebi.ac.uk/pdbsum/4xzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LEG4_HUMAN LEG4_HUMAN]] Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions.
+[https://www.uniprot.org/uniprot/LEG4_HUMAN LEG4_HUMAN] Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Galectins are proteins involved in diverse cellular contexts due to their capacity to decipher and respond to the information encoded by beta-galactoside sugars. In particular, human galectin-4, normally expressed in the healthy gastrointestinal tract, displays differential expression in cancerous tissues and is considered a potential drug target for liver and lung cancer. Galectin-4 is a tandem-repeat galectin characterized by two carbohydrate recognition domains connected by a linker-peptide. Despite their relevance to cell function and pathogenesis, structural characterization of full-length tandem-repeat galectins has remained elusive. Here, we investigate galectin-4 using X-ray crystallography, small- and wide-angle X-ray scattering, molecular modelling, molecular dynamics simulations, and differential scanning fluorimetry assays and describe for the first time a structural model for human galectin-4. Our results provide insight into the structural role of the linker-peptide and shed light on the dynamic characteristics of the mechanism of carbohydrate recognition among tandem-repeat galectins.
+Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication.,Rustiguel JK, Soares RO, Meisburger SP, Davis KM, Malzbender KL, Ando N, Dias-Baruffi M, Nonato MC Sci Rep. 2016 Sep 19;6:33633. doi: 10.1038/srep33633. PMID:27642006<ref>PMID:27642006</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4xzp" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Galectin 3D structures|Galectin 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Nonato, M C]]
+[[Category: Homo sapiens]]
-[[Category: Rustiguel, J K]]
+[[Category: Large Structures]]
-[[Category: Beta-galactosides binding]]
+[[Category: Nonato MC]]
-[[Category: Galectin]]
+[[Category: Rustiguel JK]]
-[[Category: Sugar binding protein]]