4cz5: Difference between revisions
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<StructureSection load='4cz5' size='340' side='right'caption='[[4cz5]], [[Resolution|resolution]] 1.02Å' scene=''> | <StructureSection load='4cz5' size='340' side='right'caption='[[4cz5]], [[Resolution|resolution]] 1.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cz5]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4cz5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZ5 FirstGlance]. <br> | ||
</td></tr> | </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=4cz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cz5 OCA], [https://pdbe.org/4cz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cz5 RCSB], [https://www.ebi.ac.uk/pdbsum/4cz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cz5 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/P53_DANRE P53_DANRE]] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of bax and fas antigen expression, or by repression of Bcl-2 expression.<ref>PMID:12477391</ref> <ref>PMID:15630097</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Danio rerio]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Joerger | [[Category: Joerger AC]] | ||
Revision as of 10:39, 14 September 2022
Truncated tetramerization domain of zebrafish p53 (crystal form I)Truncated tetramerization domain of zebrafish p53 (crystal form I)
Structural highlights
Function[P53_DANRE] Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of bax and fas antigen expression, or by repression of Bcl-2 expression.[1] [2] Publication Abstract from PubMedThe tetrameric transcription factors p53, p63, and p73 evolved from a common ancestor and play key roles in tumor suppression and development. Surprisingly, p63 and p73 require a second helix in their tetramerization domain for the formation of stable tetramers that is absent in human p53, raising questions about the evolutionary processes leading to diversification. Here we determined the crystal structure of the zebrafish p53 tetramerization domain, which contains a second helix, reminiscent of p63 and p73, combined with p53-like features. Through comprehensive phylogenetic analyses, we systematically traced the evolution of vertebrate p53 family oligomerization domains back to the beginning of multicellular life. We provide evidence that their last common ancestor also had an extended p63/p73-like domain and pinpoint evolutionary events that shaped this domain during vertebrate radiation. Domain compaction and transformation of a structured into a flexible, intrinsically disordered region may have contributed to the expansion of the human p53 interactome. Tracing the Evolution of the p53 Tetramerization Domain.,Joerger AC, Wilcken R, Andreeva A Structure. 2014 Sep 2;22(9):1301-10. doi: 10.1016/j.str.2014.07.010. PMID:25185827[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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