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| | <StructureSection load='2d6k' size='340' side='right'caption='[[2d6k]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2d6k' size='340' side='right'caption='[[2d6k]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2d6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D6K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2d6k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D6K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d6l|2d6l]], [[2d6m|2d6m]], [[2d6n|2d6n]], [[2d6o|2d6o]], [[2d6p|2d6p]]</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]] 2.5Å</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=2d6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6k OCA], [http://pdbe.org/2d6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d6k RCSB], [http://www.ebi.ac.uk/pdbsum/2d6k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d6k 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=2d6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6k OCA], [https://pdbe.org/2d6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d6k RCSB], [https://www.ebi.ac.uk/pdbsum/2d6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d6k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LEG9_MOUSE LEG9_MOUSE]] Binds galactosides. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death (By similarity). | + | [https://www.uniprot.org/uniprot/LEG9_MOUSE LEG9_MOUSE] Binds galactosides. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kato, R]] | + | [[Category: Kato R]] |
| - | [[Category: Murata, T]] | + | [[Category: Murata T]] |
| - | [[Category: Nagae, M]] | + | [[Category: Nagae M]] |
| - | [[Category: Nakamura, T]] | + | [[Category: Nakamura T]] |
| - | [[Category: Nishi, N]] | + | [[Category: Nishi N]] |
| - | [[Category: Wakatsuki, S]] | + | [[Category: Wakatsuki S]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Carbohydrate binding protein]]
| + | |
| - | [[Category: Galectin]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Sugar binding protein]]
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| Structural highlights
Function
LEG9_MOUSE Binds galactosides. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death (By similarity).
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
The galectins are a family of beta-galactoside-binding animal lectins with a conserved carbohydrate recognition domain (CRD). They have a high affinity for small beta-galactosides, but binding specificity for complex glycoconjugates varies considerably within the family. The ligand recognition is essential for their proper function, and the structures of several galectins have suggested their mechanism of carbohydrate binding. Galectin-9 has two tandem CRDs with a short linker, and we report the crystal structures of mouse galectin-9 N-terminal CRD (NCRD) in the absence and the presence of four ligand complexes. All structures form the same dimer, which is quite different from the canonical 2-fold symmetric dimer seen for galectin-1 and -2. The beta-galactoside recognition mechanism in the galectin-9 NCRD is highly conserved among other galectins. In the apo form structure, water molecules mimic the ligand hydrogen-bond network. The galectin-9 NCRD can bind both N-acetyllactosamine (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of Arg-64. Moreover, the structure of the N-acetyllactosamine dimer (Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc) complex shows a unique binding mode of galectin-9. Finally, surface plasmon resonance assay showed that the galectin-9 NCRD forms a homophilic dimer not only in the crystal but also in solution.
Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition.,Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R J Biol Chem. 2006 Nov 24;281(47):35884-93. Epub 2006 Sep 21. PMID:16990264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R. Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition. J Biol Chem. 2006 Nov 24;281(47):35884-93. Epub 2006 Sep 21. PMID:16990264 doi:http://dx.doi.org/10.1074/jbc.M606648200
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