2dwv: Difference between revisions
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New page: left|200px<br /><applet load="2dwv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dwv" /> '''Solution structure of the second WW domain f... |
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== | ==Solution structure of the second WW domain from mouse salvador homolog 1 protein (mWW45)== | ||
The WW domain is known as one of the smallest protein modules with a | <StructureSection load='2dwv' size='340' side='right'caption='[[2dwv]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2dwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DWV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2dwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dwv OCA], [https://pdbe.org/2dwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dwv RCSB], [https://www.ebi.ac.uk/pdbsum/2dwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dwv ProSAT], [https://www.topsan.org/Proteins/RSGI/2dwv TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAV1_MOUSE SAV1_MOUSE] Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation (By similarity).<ref>PMID:18369314</ref> <ref>PMID:20080689</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/2dwv_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dwv ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The WW domain is known as one of the smallest protein modules with a triple-stranded beta-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a beta-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the beta-sheet, this WW domain buries these residues in the dimer interface. | |||
Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form.,Ohnishi S, Guntert P, Koshiba S, Tomizawa T, Akasaka R, Tochio N, Sato M, Inoue M, Harada T, Watanabe S, Tanaka A, Shirouzu M, Kigawa T, Yokoyama S FEBS Lett. 2007 Feb 6;581(3):462-8. Epub 2007 Jan 16. PMID:17239860<ref>PMID:17239860</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2dwv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Guntert P]] | |||
[[Category: Guntert | [[Category: Harada T]] | ||
[[Category: Harada | [[Category: Inoue M]] | ||
[[Category: Inoue | [[Category: Kigawa T]] | ||
[[Category: Kigawa | [[Category: Koshiba S]] | ||
[[Category: Koshiba | [[Category: Ohnishi S]] | ||
[[Category: Ohnishi | [[Category: Sato M]] | ||
[[Category: Tochio N]] | |||
[[Category: Sato | [[Category: Tomizawa T]] | ||
[[Category: Tochio | [[Category: Watanabe S]] | ||
[[Category: Tomizawa | [[Category: Yokoyama S]] | ||
[[Category: Watanabe | |||
[[Category: Yokoyama | |||
