7bqf: Difference between revisions

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'''Unreleased structure'''


The entry 7bqf is ON HOLD
==Dimerization of SAV1 WW tandem==
<StructureSection load='7bqf' size='340' side='right'caption='[[7bqf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BQF 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]] 1.7003762&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</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=7bqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqf OCA], [https://pdbe.org/7bqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bqf RCSB], [https://www.ebi.ac.uk/pdbsum/7bqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqf ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The canonical mammalian Hippo pathway contains a core kinase signaling cascade requiring upstream MST to form a stable complex with SAV1 in order to phosphorylate the downstream LATS/MOB complex. Though SAV1 dimerization is essential for the trans-activation of MST, the molecular mechanism underlying SAV1 dimerization is unclear. Here, we discover that the SAV1 WW tandem containing a short Pro-rich extension immediately following the WW tandem (termed as "WW12ex") forms a highly stable homodimer. The crystal structure of SAV1 WW12ex reveals that the Pro-rich extension of one subunit binds to both WW domains from the other subunit. Thus, SAV1 WW12ex forms a domain-swapped dimer instead of a WW2 homodimerization-mediated dimer. The WW12ex-mediated dimerization of SAV1 is required for the MST/SAV1 complex assembly and MST kinase activation. Finally, we show that several cancer-related SAV1 variants disrupt SAV1 dimer formation, and thus, these mutations may impair the tumor-suppression activity of SAV1.


Authors: Lin, Z., Zhang, M.
A WW Tandem-Mediated Dimerization Mode of SAV1 Essential for Hippo Signaling.,Lin Z, Xie R, Guan K, Zhang M Cell Rep. 2020 Sep 8;32(10):108118. doi: 10.1016/j.celrep.2020.108118. PMID:32905778<ref>PMID:32905778</ref>


Description: Dimerization of SAV1 WW tandem
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Lin, Z]]
<div class="pdbe-citations 7bqf" style="background-color:#fffaf0;"></div>
[[Category: Zhang, M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lin Z]]
[[Category: Zhang M]]
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