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| | <StructureSection load='2zkn' size='340' side='right'caption='[[2zkn]], [[Resolution|resolution]] 1.86Å' scene=''> | | <StructureSection load='2zkn' size='340' side='right'caption='[[2zkn]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zkn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZKN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zkn]] 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=2ZKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZKN FirstGlance]. <br> |
| - | </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></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]] 1.86Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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></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=2zkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zkn OCA], [https://pdbe.org/2zkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zkn RCSB], [https://www.ebi.ac.uk/pdbsum/2zkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zkn ProSAT]</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=2zkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zkn OCA], [https://pdbe.org/2zkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zkn RCSB], [https://www.ebi.ac.uk/pdbsum/2zkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zkn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LEG1_HUMAN LEG1_HUMAN]] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.<ref>PMID:14617626</ref> <ref>PMID:18796645</ref>
| + | [https://www.uniprot.org/uniprot/LEG1_HUMAN LEG1_HUMAN] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.<ref>PMID:14617626</ref> <ref>PMID:18796645</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abe, A]] | + | [[Category: Abe A]] |
| - | [[Category: Kamitori, S]] | + | [[Category: Kamitori S]] |
| - | [[Category: Yoshida, H]] | + | [[Category: Yoshida H]] |
| - | [[Category: Acetylation]]
| + | |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Lectin]]
| + | |
| Structural highlights
Function
LEG1_HUMAN May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.[1] [2]
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-1 (Gal-1), a member of the beta-galactoside-binding animal lectin family, has a wide range of biological activities, which makes it an attractive target for medical applications. Unlike other galectins, Gal-1 is susceptible to oxidation at cysteine residues, which is troublesome for in vitro/vivo studies. To overcome this problem, we prepared a cysteine-less mutant of Gal-1 (CSGal-1) by substituting all cysteine residues with serine residues. In the case of wild-type Gal-1, the formation of covalent dimers/oligomers was evident after 10 days of storage in the absence of a reducing agent with a concomitant decrease in hemagglutination activity, while CSGal-1 did not form multimers and retained full hemagglutination activity after 400 days of storage. Frontal affinity chromatography showed that the sugar-binding specificity and affinity of Gal-1 for model glycans were barely affected by the mutagenesis. Gal-1 is known to induce cell signaling leading to an increase in the intracytoplasmic calcium concentration and to cell death. CSGal-1 is also capable of inducing calcium flux and growth inhibition in Jurkat cells, which are comparable to or more potent than those induced by Gal-1. The X-ray structure of the CSGal-1/lactose complex has been determined. The structure of CSGal-1 is almost identical to that of wild-type human Gal-1, showing that the amino acid substitutions do not affect the overall structure or carbohydrate-binding site structure of the protein. These results indicate that CSGal-1 can serve as a stable substitute for Gal-1.
Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1.,Nishi N, Abe A, Iwaki J, Yoshida H, Itoh A, Shoji H, Kamitori S, Hirabayashi J, Nakamura T Glycobiology. 2008 Dec;18(12):1065-73. Epub 2008 Sep 16. PMID:18796645[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ He J, Baum LG. Presentation of galectin-1 by extracellular matrix triggers T cell death. J Biol Chem. 2004 Feb 6;279(6):4705-12. Epub 2003 Nov 14. PMID:14617626 doi:10.1074/jbc.M311183200
- ↑ Nishi N, Abe A, Iwaki J, Yoshida H, Itoh A, Shoji H, Kamitori S, Hirabayashi J, Nakamura T. Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. Glycobiology. 2008 Dec;18(12):1065-73. Epub 2008 Sep 16. PMID:18796645 doi:10.1093/glycob/cwn089
- ↑ Nishi N, Abe A, Iwaki J, Yoshida H, Itoh A, Shoji H, Kamitori S, Hirabayashi J, Nakamura T. Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. Glycobiology. 2008 Dec;18(12):1065-73. Epub 2008 Sep 16. PMID:18796645 doi:10.1093/glycob/cwn089
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