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| | <StructureSection load='2qmq' size='340' side='right'caption='[[2qmq]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2qmq' size='340' side='right'caption='[[2qmq]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qmq]] is a 1 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=2QMQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QMQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qmq]] is a 1 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=2QMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">15277975, Ndrg2, Kiaa1248, Ndr2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2qmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmq OCA], [http://pdbe.org/2qmq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qmq RCSB], [http://www.ebi.ac.uk/pdbsum/2qmq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmq ProSAT], [http://www.topsan.org/Proteins/JCSG/2qmq TOPSAN]</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=2qmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmq OCA], [https://pdbe.org/2qmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmq RCSB], [https://www.ebi.ac.uk/pdbsum/2qmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmq ProSAT], [https://www.topsan.org/Proteins/JCSG/2qmq TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NDRG2_MOUSE NDRG2_MOUSE]] Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (By similarity). | + | [https://www.uniprot.org/uniprot/NDRG2_MOUSE NDRG2_MOUSE] Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (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: Structural genomic]]
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| - | [[Category: Alpha/beta-hydrolases fold]]
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| - | [[Category: Developmental protein]]
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| - | [[Category: Differentiation]]
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| - | [[Category: Jcsg]]
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| - | [[Category: Ndr family]]
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| - | [[Category: Neurogenesis]]
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| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Regulatory protein]]
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| - | [[Category: Signaling protein]]
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| Structural highlights
Function
NDRG2_MOUSE Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation (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
Considerable attention has recently been paid to the N-Myc downstream-regulated gene (NDRG) family because of its potential as a tumor suppressor in many human cancers. Primary amino-acid sequence information suggests that the NDRG family proteins may belong to alpha/beta hydrolase superfamily; however, their functional role has not yet been determined. Here, we present the crystal structures of the human and mouse NDRG2 proteins determined at 2.0 and 1.7 Angstrom resolution, respectively. Both NDRG2 proteins show remarkable structural similarity to the alpha/beta hydrolase superfamily of proteins, despite limited sequence similarity. Structural analysis suggests that NDRG2 is a non-enzymatic member of the alpha/beta hydrolase superfamily, since it lacks the catalytic signature residues and has an occluded substrate-binding site. Several conserved structural features suggest NDRG may be involved in molecular interactions. Mutagenesis data based on the structural analysis support a crucial role for helix alpha6 in the suppression of TCF/beta-catenin signaling in the tumorigenesis of human colorectal cancer, via a molecular interaction.
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor.,Hwang J, Kim Y, Kang HB, Jaroszewski L, Deacon A, Lee H, Choi WC, Kim KJ, Kim CH, Kang BS, Lee JO, Oh TK, Kim JW, Wilson IA, Kim MH J Biol Chem. 2011 Jan 18. PMID:21247902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hwang J, Kim Y, Kang HB, Jaroszewski L, Deacon A, Lee H, Choi WC, Kim KJ, Kim CH, Kang BS, Lee JO, Oh TK, Kim JW, Wilson IA, Kim MH. Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor. J Biol Chem. 2011 Jan 18. PMID:21247902 doi:10.1074/jbc.M110.170803
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