4xzp
From Proteopedia
(Difference between revisions)
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</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cbl|5cbl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cbl|5cbl]]</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'>[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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzp ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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. | [[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. | ||
| + | <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> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:44, 19 October 2016
Crystal structure of the N-terminal domain of human galectin-4
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