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4qmg

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'''Unreleased structure'''
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==The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions==
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<StructureSection load='4qmg' size='340' side='right' caption='[[4qmg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4qmg]] is a 10 chain structure. 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>
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</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>
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<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>
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<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>
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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=4qmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qmg RCSB], [http://www.ebi.ac.uk/pdbsum/4qmg 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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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.
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The entry 4qmg is ON HOLD
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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<ref>PMID:25242325</ref>
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Authors: Xing, Y., Guo, F., Kang, Y., Satyshur, K.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions
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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: Guo, F.]]
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[[Category: Kang, Y.]]
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[[Category: Satyshur, K.]]
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[[Category: Stanevich, V.]]
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[[Category: Wan, L.]]
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[[Category: Xing, Y.]]
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[[Category: Breast cancer]]
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[[Category: Dna/rna-binding]]
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[[Category: Mirna-mediated silencing]]
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[[Category: Mtdh]]
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[[Category: Nuclease]]
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[[Category: Sn domain]]
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[[Category: Snd1]]
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[[Category: Transcription]]
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[[Category: Tumorigenesis]]

Revision as of 07:35, 8 October 2014

The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions

4qmg, resolution 2.70Å

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