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| - | ==Crystal structure of MAGEG1 and NSE1 complex==
| + | #REDIRECT [[5wy5]] This PDB entry is obsolete and replaced by 5wy5 |
| - | <StructureSection load='3nw0' size='340' side='right' caption='[[3nw0]], [[Resolution|resolution]] 2.92Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[3nw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NW0 FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HCA4, MAGEG1, NDNL2, NSMCE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), HSPC333, HSPC337, NDNL2, NSMCE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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| - | <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=3nw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3nw0 PDBsum]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The melanoma antigen (MAGE) family consists of more than 60 genes, many of which are cancer-testis antigens that are highly expressed in cancer and play a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive. Here, we identify really interesting new gene (RING) domain proteins as binding partners for MAGE family proteins. Multiple MAGE family proteins bind E3 RING ubiquitin ligases with specificity. The crystal structure of one of these MAGE-RING complexes, MAGE-G1-NSE1, reveals structural insights into MAGE family proteins and their interaction with E3 RING ubiquitin ligases. Biochemical and cellular assays demonstrate that MAGE proteins enhance the ubiquitin ligase activity of RING domain proteins. For example, MAGE-C2-TRIM28 is shown to target p53 for degradation in a proteasome-dependent manner, consistent with its tumorigenic functions. These findings define a biochemical and cellular function for the MAGE protein family.
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| - | MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.,Doyle JM, Gao J, Wang J, Yang M, Potts PR Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041<ref>PMID:20864041</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Homo sapiens]]
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| - | [[Category: Gao, J]]
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| - | [[Category: Yang, M]]
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| - | [[Category: E3 ligase]]
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| - | [[Category: Metal binding protein]]
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| - | [[Category: Zn]]
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