2mw4: Difference between revisions

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'''Unreleased structure'''
==Tetramerization domain of the Ciona intestinalis p53/p73-b transcription factor protein==
<StructureSection load='2mw4' size='340' side='right' caption='[[2mw4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mw4]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MW4 FirstGlance]. <br>
</td></tr><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=2mw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw4 OCA], [http://pdbe.org/2mw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mw4 RCSB], [http://www.ebi.ac.uk/pdbsum/2mw4 PDBsum]</span></td></tr>
</table>
<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.


The entry 2mw4 is ON HOLD  until Paper Publication
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>


Authors: Heering, J.P., Jonker, H.R.A., Loehr, F., Schwalbe, H., Doetsch, V.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Tetramerization domain of the Ciona intestinalis p53/p73-b transcription factor protein
<div class="pdbe-citations 2mw4" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Doetsch, V]]
[[Category: Doetsch, V]]
[[Category: Jonker, H.R.A]]
[[Category: Heering, J P]]
[[Category: Jonker, H R.A]]
[[Category: Loehr, F]]
[[Category: Schwalbe, H]]
[[Category: Schwalbe, H]]
[[Category: Heering, J.P]]
[[Category: Ciona intestinali]]
[[Category: Loehr, F]]
[[Category: P53/p73-b]]
[[Category: Tetramerization domain]]
[[Category: Transcription]]
[[Category: Transcription factor]]
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