2qmq
From Proteopedia
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| - | [[Image:2qmq.jpg|left|200px]] | ||
| - | + | ==Crystal structure of a n-myc downstream regulated 2 protein (ndrg2, syld, ndr2, ai182517, au040374) from mus musculus at 1.70 A resolution== | |
| - | + | <StructureSection load='2qmq' size='340' side='right'caption='[[2qmq]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <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='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='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'>[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> | |
| - | + | == Function == | |
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qm/2qmq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qmq ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21247902</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | == | + | </div> |
| - | + | <div class="pdbe-citations 2qmq" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Single protein]] | ||
| - | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
| - | [[Category: 15277975]] | ||
| - | [[Category: alternative splicing]] | ||
| - | [[Category: cytoplasm]] | ||
| - | [[Category: developmental protein]] | ||
| - | [[Category: differentiation]] | ||
| - | [[Category: jcsg]] | ||
| - | [[Category: joint center for structural genomic]] | ||
| - | [[Category: n-myc downstream regulated 2]] | ||
| - | [[Category: ndr family]] | ||
| - | [[Category: neurogenesis]] | ||
| - | [[Category: phosphorylation]] | ||
| - | [[Category: protein structure initiative]] | ||
| - | [[Category: psi-2]] | ||
| - | [[Category: regulatory protein]] | ||
| - | [[Category: signaling protein]] | ||
| - | [[Category: structural genomic]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 25 23:34:50 2008'' | ||
Current revision
Crystal structure of a n-myc downstream regulated 2 protein (ndrg2, syld, ndr2, ai182517, au040374) from mus musculus at 1.70 A resolution
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