4xzp: Difference between revisions
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==Crystal structure of the N-terminal domain of human galectin-4== | ==Crystal structure of the N-terminal domain of human galectin-4== | ||
<StructureSection load='4xzp' size='340' side='right' caption='[[4xzp]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='4xzp' size='340' side='right'caption='[[4xzp]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == 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 [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> | ||
<tr id=' | <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'>[ | <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> | </table> | ||
== Function == | == Function == | ||
[ | [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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Nonato MC]] | ||
[[Category: | [[Category: Rustiguel JK]] | ||
Latest revision as of 10:52, 27 September 2023
Crystal structure of the N-terminal domain of human galectin-4Crystal structure of the N-terminal domain of human galectin-4
Structural highlights
FunctionLEG4_HUMAN Galectin that binds lactose and a related range of sugars. May be involved in the assembly of adherens junctions. Publication Abstract from PubMedGalectins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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