View source for 2mw4


==Tetramerization domain of the Ciona intestinalis p53/p73-b transcription factor protein==
<StructureSection load='2mw4' size='340' side='right'caption='[[2mw4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mw4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ciona_intestinalis Ciona intestinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MW4 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=2mw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw4 OCA], [https://pdbe.org/2mw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mw4 RCSB], [https://www.ebi.ac.uk/pdbsum/2mw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F6SSG7_CIOIN F6SSG7_CIOIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Most members of the p53 family of transcription factors form tetramers. Responsible for determining the oligomeric state is a short oligomerization domain consisting of one beta-strand and one alpha-helix. With the exception of human p53 all other family members investigated so far contain a second alpha-helix as part of their tetramerization domain. Here we have used nuclear magnetic resonance spectroscopy to characterize the oligomerization domains of the two p53-like proteins from the tunicate Ciona intestinalis, representing the closest living relative of vertebrates. Structure determination reveals for one of the two proteins a new type of packing of this second alpha-helix on the core domain that was not predicted based on the sequence, while the other protein does not form a second helix despite the presence of crucial residues that are conserved in all other family members that form a second helix. By mutational analysis, we identify a proline as well as large hydrophobic residues in the hinge region between both helices as the crucial determinant for the formation of a second helix.

Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain.,Heering J, Jonker HR, Lohr F, Schwalbe H, Dotsch V Protein Sci. 2016 Feb;25(2):410-22. doi: 10.1002/pro.2830. Epub 2015 Nov 25. PMID:26473758<ref>PMID:26473758</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mw4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Ciona intestinalis]]
[[Category: Large Structures]]
[[Category: Doetsch V]]
[[Category: Heering JP]]
[[Category: Jonker HRA]]
[[Category: Loehr F]]
[[Category: Schwalbe H]]