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4guq

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==Structure of mutS139F p73 DNA binding domain complexed with 20BP DNA response element==
==Structure of mutS139F p73 DNA binding domain complexed with 20BP DNA response element==
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<StructureSection load='4guq' size='340' side='right' caption='[[4guq]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
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<StructureSection load='4guq' size='340' side='right'caption='[[4guq]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4guq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GUQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4guq]] is a 4 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=4GUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GUQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g82|4g82]], [[4g83|4g83]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">human p73, P73, TP73 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4guq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4guq OCA], [https://pdbe.org/4guq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4guq RCSB], [https://www.ebi.ac.uk/pdbsum/4guq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4guq ProSAT]</span></td></tr>
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<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=4guq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4guq OCA], [http://pdbe.org/4guq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4guq RCSB], [http://www.ebi.ac.uk/pdbsum/4guq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4guq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Structural and biochemical studies have demonstrated that p73, p63 and p53 recognize DNA with identical amino acids and similar binding affinity. Here, measuring transactivation activity for a large number of response elements (REs) in yeast and human cell lines, we show that p53 family proteins also have overlapping transactivation profiles. We identified mutations at conserved amino acids of loops L1 and L3 in the DNA-binding domain that tune the transactivation potential nearly equally in p73, p63 and p53. For example, the mutant S139F in p73 has higher transactivation potential towards selected REs, enhanced DNA-binding cooperativity in vitro and a flexible loop L1 as seen in the crystal structure of the protein-DNA complex. By studying, how variations in the RE sequence affect transactivation specificity, we discovered a RE-transactivation code that predicts enhanced transactivation; this correlation is stronger for promoters of genes associated with apoptosis.
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Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code.,Ciribilli Y, Monti P, Bisio A, Nguyen HT, Ethayathulla AS, Ramos A, Foggetti G, Menichini P, Menendez D, Resnick MA, Viadiu H, Fronza G, Inga A Nucleic Acids Res. 2013 Jul 26. PMID:23892287<ref>PMID:23892287</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4guq" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Ethayathulla, A S]]
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[[Category: Large Structures]]
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[[Category: Nguyen, H T]]
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[[Category: Ethayathulla AS]]
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[[Category: Viadiu, H]]
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[[Category: Nguyen HT]]
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[[Category: Beta-immunoglobulin]]
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[[Category: Viadiu H]]
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[[Category: Transcription factor]]
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[[Category: Transcription-dna complex]]
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[[Category: Tumor suppressor]]
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Current revision

Structure of mutS139F p73 DNA binding domain complexed with 20BP DNA response element

PDB ID 4guq

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