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| | <StructureSection load='4qmg' size='340' side='right'caption='[[4qmg]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4qmg' size='340' side='right'caption='[[4qmg]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qmg]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QMG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qmg]] is a 10 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=4QMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QMG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4qmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmg OCA], [https://pdbe.org/4qmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qmg RCSB], [https://www.ebi.ac.uk/pdbsum/4qmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qmg ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3omc|3omc]], [[2e6n|2e6n]], [[3omg|3omg]], [[3bdl|3bdl]], [[2hqe|2hqe]], [[2hqx|2hqx]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Metadherin (MTDH) and Staphylococcal nuclease domain containing 1 (SND1), SND1, TDRD11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), AEG1, LYRIC, Metadherin (MTDH), MTDH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4qmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmg OCA], [http://pdbe.org/4qmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qmg RCSB], [http://www.ebi.ac.uk/pdbsum/4qmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qmg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SND1_HUMAN SND1_HUMAN]] Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).<ref>PMID:7651391</ref> [[http://www.uniprot.org/uniprot/LYRIC_HUMAN LYRIC_HUMAN]] Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance.<ref>PMID:15927426</ref> <ref>PMID:16452207</ref> <ref>PMID:18316612</ref> <ref>PMID:19111877</ref> | + | [https://www.uniprot.org/uniprot/SND1_HUMAN SND1_HUMAN] Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).<ref>PMID:7651391</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, F]] | + | [[Category: Guo F]] |
| - | [[Category: Kang, Y]] | + | [[Category: Kang Y]] |
| - | [[Category: Satyshur, K]] | + | [[Category: Satyshur K]] |
| - | [[Category: Stanevich, V]] | + | [[Category: Stanevich V]] |
| - | [[Category: Wan, L]] | + | [[Category: Wan L]] |
| - | [[Category: Xing, Y]] | + | [[Category: Xing Y]] |
| - | [[Category: Breast cancer]]
| + | |
| - | [[Category: Dna/rna-binding]]
| + | |
| - | [[Category: Mirna-mediated silencing]]
| + | |
| - | [[Category: Mtdh]]
| + | |
| - | [[Category: Nuclease]]
| + | |
| - | [[Category: Sn domain]]
| + | |
| - | [[Category: Snd1]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Tumorigenesis]]
| + | |
| Structural highlights
Function
SND1_HUMAN Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Functions as a transcriptional coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).[1]
Publication Abstract from PubMed
Metadherin (MTDH) and Staphylococcal nuclease domain containing 1 (SND1) are overexpressed and interact in diverse cancer types. The structural mechanism of their interaction remains unclear. Here, we determined the high-resolution crystal structure of MTDH-SND1 complex, which reveals an 11-residue MTDH peptide motif occupying an extended protein groove between two SN domains (SN1/2), with two MTDH tryptophan residues nestled into two well-defined pockets in SND1. At the opposite side of the MTDH-SND1 binding interface, SND1 possesses long protruding arms and deep surface valleys that are prone to binding with other partners. Despite the simple binding mode, interactions at both tryptophan-binding pockets are important for MTDH and SND1's roles in breast cancer and for SND1 stability under stress. Our study reveals a unique mode of interaction with SN domains that dictates cancer-promoting activity and provides a structural basis for mechanistic understanding of MTDH-SND1-mediated signaling and for exploring therapeutic targeting of this complex.
Structural Insights into the Tumor-Promoting Function of the MTDH-SND1 Complex.,Guo F, Wan L, Zheng A, Stanevich V, Wei Y, Satyshur KA, Shen M, Lee W, Kang Y, Xing Y Cell Rep. 2014 Sep 25;8(6):1704-13. doi: 10.1016/j.celrep.2014.08.033. Epub 2014 , Sep 18. PMID:25242325[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tong X, Drapkin R, Yalamanchili R, Mosialos G, Kieff E. The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. Mol Cell Biol. 1995 Sep;15(9):4735-44. PMID:7651391
- ↑ Guo F, Wan L, Zheng A, Stanevich V, Wei Y, Satyshur KA, Shen M, Lee W, Kang Y, Xing Y. Structural Insights into the Tumor-Promoting Function of the MTDH-SND1 Complex. Cell Rep. 2014 Sep 25;8(6):1704-13. doi: 10.1016/j.celrep.2014.08.033. Epub 2014 , Sep 18. PMID:25242325 doi:http://dx.doi.org/10.1016/j.celrep.2014.08.033
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