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| | ==Crystal structure of human galectin-3 carbohydrate-recognition domain with lactose bound, at 1.35 angstrom resolution== | | ==Crystal structure of human galectin-3 carbohydrate-recognition domain with lactose bound, at 1.35 angstrom resolution== |
| - | <StructureSection load='2nn8' size='340' side='right' caption='[[2nn8]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='2nn8' size='340' side='right'caption='[[2nn8]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NN8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NN8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2NN8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene>, <scene name='pdbligand=LBT:ALPHA-LACTOSE'>LBT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene>, <scene name='pdbligand=LBT:ALPHA-LACTOSE'>LBT</scene></td></tr> |
| | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nmn|2nmn]], [[2nmo|2nmo]]</td></tr> | | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nmn|2nmn]], [[2nmo|2nmo]]</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=2nn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nn8 OCA], [http://pdbe.org/2nn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nn8 RCSB], [http://www.ebi.ac.uk/pdbsum/2nn8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nn8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2nn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nn8 OCA], [http://pdbe.org/2nn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nn8 RCSB], [http://www.ebi.ac.uk/pdbsum/2nn8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nn8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | ==See Also== | | ==See Also== |
| - | *[[Galectin|Galectin]] | + | *[[Galectin 3D structures|Galectin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Blanchard, H]] | | [[Category: Blanchard, H]] |
| | [[Category: Collins, P M]] | | [[Category: Collins, P M]] |
| | [[Category: Beta-sandwich]] | | [[Category: Beta-sandwich]] |
| | [[Category: Sugar binding protein]] | | [[Category: Sugar binding protein]] |
| Structural highlights
Function
[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.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Galectin-3 is a multifunctional carbohydrate-binding protein that has roles in cancer progression. In addition to carbohydrate-dependent extracellular functions, galectin-3 participates in carbohydrate-independent intracellular signalling pathways, including apoptosis, via protein-protein interactions, some of which engage the carbohydrate-binding groove. When ligands bind within this site, conformational rearrangements are induced and information on unliganded galectin-3 is therefore valuable for structure-based drug design. Removal of cocrystallized lactose from the human galectin-3 carbohydrate-recognition domain was achieved via crystal soaking, but took weeks despite low affinity. Pre-soaking to remove lactose enabled the subsequent binding of cryoprotectant glycerol, whereas when the lactose was not removed a priori the glycerol could not displace it in the short cryosoaking time frame. This slow diffusion of lactose out of the crystals contrasts with the entrance of glycerol, which takes place within minutes. The importance of the removal of incumbent ligands prior to attempts to introduce alternative ligands is indicated, even for proteins exhibiting low affinity for ligands, and has significance for ligand exchange in structure-based drug design.
Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocols.,Collins PM, Hidari KI, Blanchard H Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):415-9. Epub 2007, Feb 21. PMID:17327679[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fukushi J, Makagiansar IT, Stallcup WB. NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin. Mol Biol Cell. 2004 Aug;15(8):3580-90. Epub 2004 Jun 4. PMID:15181153 doi:http://dx.doi.org/10.1091/mbc.E04-03-0236
- ↑ Henderson NC, Sethi T. The regulation of inflammation by galectin-3. Immunol Rev. 2009 Jul;230(1):160-71. doi: 10.1111/j.1600-065X.2009.00794.x. PMID:19594635 doi:10.1111/j.1600-065X.2009.00794.x
- ↑ Haudek KC, Spronk KJ, Voss PG, Patterson RJ, Wang JL, Arnoys EJ. Dynamics of galectin-3 in the nucleus and cytoplasm. Biochim Biophys Acta. 2010 Feb;1800(2):181-189. Epub 2009 Jul 16. PMID:19616076 doi:S0304-4165(09)00194-9
- ↑ Collins PM, Hidari KI, Blanchard H. Slow diffusion of lactose out of galectin-3 crystals monitored by X-ray crystallography: possible implications for ligand-exchange protocols. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):415-9. Epub 2007, Feb 21. PMID:17327679 doi:http://dx.doi.org/10.1107/S090744490605270X
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