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<StructureSection load='3vd0' size='340' side='right'caption='[[3vd0]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
<StructureSection load='3vd0' size='340' side='right'caption='[[3vd0]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vd0]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VD0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3vd0]] is a 16 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=3VD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VD0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vd1|3vd1]], [[3vd2|3vd2]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3vd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vd0 OCA], [https://pdbe.org/3vd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vd0 RCSB], [https://www.ebi.ac.uk/pdbsum/3vd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vd0 ProSAT]</span></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=3vd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vd0 OCA], [https://pdbe.org/3vd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vd0 RCSB], [https://www.ebi.ac.uk/pdbsum/3vd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vd0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/P73_HUMAN P73_HUMAN]] Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein.<ref>PMID:11753569</ref> <ref>PMID:10203277</ref> <ref>PMID:18174154</ref> 
[https://www.uniprot.org/uniprot/P73_HUMAN P73_HUMAN] Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein.<ref>PMID:11753569</ref> <ref>PMID:10203277</ref> <ref>PMID:18174154</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The transcription factor p73 triggers developmental pathways and overlaps stress-induced p53 transcriptional pathways. How p53-family response elements determine and regulate transcriptional specificity remains an unsolved problem. In this work, we have determined the first crystal structures of p73 DNA-binding domain tetramer bound to response elements with spacers of different length. The structure and function of the adaptable tetramer are determined by the distance between two half-sites. The structures with zero and one base-pair spacers show compact p73 DNA-binding domain tetramers with large tetramerization interfaces; a two base-pair spacer results in DNA unwinding and a smaller tetramerization interface, whereas a four base-pair spacer hinders tetramerization. Functionally, p73 is more sensitive to spacer length than p53, with one base-pair spacer reducing 90% of transactivation activity and longer spacers reducing transactivation to basal levels. Our results establish the quaternary structure of the p73 DNA-binding domain required as a scaffold to promote transactivation.
 
Structure of p73 DNA-binding domain tetramer modulates p73 transactivation.,Ethayathulla AS, Tse PW, Monti P, Nguyen S, Inga A, Fronza G, Viadiu H Proc Natl Acad Sci U S A. 2012 Apr 2. PMID:22474346<ref>PMID:22474346</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vd0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ethayathulla, A S]]
[[Category: Ethayathulla AS]]
[[Category: Nguyen, S]]
[[Category: Nguyen S]]
[[Category: Tse, P W]]
[[Category: Tse PW]]
[[Category: Viadiu, H]]
[[Category: Viadiu H]]
[[Category: Antitumor protein-dna complex]]
[[Category: Beta-immunoglobulin-like fold]]
[[Category: Dna]]
[[Category: Protein dna complex]]
[[Category: Tumour suppressor]]

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