4qmg: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 4qmg is ON HOLD Authors: Xing, Y., Guo, F., Kang, Y., Satyshur, K. Description: The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting I... |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions== | ||
<StructureSection load='4qmg' size='340' side='right'caption='[[4qmg]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.701Å</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='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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:25242325</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4qmg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Guo F]] | |||
[[Category: Kang Y]] | |||
[[Category: Satyshur K]] | |||
[[Category: Stanevich V]] | |||
[[Category: Wan L]] | |||
[[Category: Xing Y]] | |||
Latest revision as of 03:28, 21 November 2024
The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions
| ||||||||||||
