2rp5
From Proteopedia
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| - | < | + | ==Solution structure of the oligomerization domain in CEP-1== |
| - | + | <StructureSection load='2rp5' size='340' side='right'caption='[[2rp5]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2rp5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RP5 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=2rp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rp5 OCA], [https://pdbe.org/2rp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rp5 RCSB], [https://www.ebi.ac.uk/pdbsum/2rp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rp5 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/CEP1_CAEEL CEP1_CAEEL] Transcriptional activator that binds the same DNA consensus sequence as p53. Has a role in normal development to ensure proper meiotic chromosome segregation. Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation. However, not required for DNA repair in response to UV-C or to regulate cell-cycle progression. Required for induction of ced-13 in response to DNA damage. Regulates germline proliferation by activating phg-1.<ref>PMID:11696333</ref> <ref>PMID:11557844</ref> <ref>PMID:12445383</ref> <ref>PMID:15273685</ref> <ref>PMID:15707894</ref> <ref>PMID:15605074</ref> <ref>PMID:16319925</ref> <ref>PMID:17276923</ref> <ref>PMID:17186023</ref> <ref>PMID:17347667</ref> <ref>PMID:17895432</ref> <ref>PMID:18627611</ref> <ref>PMID:18836529</ref> <ref>PMID:19015549</ref> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | |
The tetrameric state of p53, p63, and p73 has been considered one of the hallmarks of this protein family. While the DNA binding domain (DBD) is highly conserved among vertebrates and invertebrates, sequences C-terminal to the DBD are highly divergent. In particular, the oligomerization domain (OD) of the p53 forms of the model organisms Caenorhabditis elegans and Drosophila cannot be identified by sequence analysis. Here, we present the solution structures of their ODs and show that they both differ significantly from each other as well as from human p53. CEP-1 contains a composite domain of an OD and a sterile alpha motif (SAM) domain, and forms dimers instead of tetramers. The Dmp53 structure is characterized by an additional N-terminal beta-strand and a C-terminal helix. Truncation analysis in both domains reveals that the additional structural elements are necessary to stabilize the structure of the OD, suggesting a new function for the SAM domain. Furthermore, these structures show a potential path of evolution from an ancestral dimeric form over a tetrameric form, with additional stabilization elements, to the tetramerization domain of mammalian p53. | The tetrameric state of p53, p63, and p73 has been considered one of the hallmarks of this protein family. While the DNA binding domain (DBD) is highly conserved among vertebrates and invertebrates, sequences C-terminal to the DBD are highly divergent. In particular, the oligomerization domain (OD) of the p53 forms of the model organisms Caenorhabditis elegans and Drosophila cannot be identified by sequence analysis. Here, we present the solution structures of their ODs and show that they both differ significantly from each other as well as from human p53. CEP-1 contains a composite domain of an OD and a sterile alpha motif (SAM) domain, and forms dimers instead of tetramers. The Dmp53 structure is characterized by an additional N-terminal beta-strand and a C-terminal helix. Truncation analysis in both domains reveals that the additional structural elements are necessary to stabilize the structure of the OD, suggesting a new function for the SAM domain. Furthermore, these structures show a potential path of evolution from an ancestral dimeric form over a tetrameric form, with additional stabilization elements, to the tetramerization domain of mammalian p53. | ||
| - | + | Structural evolution of C-terminal domains in the p53 family.,Ou HD, Lohr F, Vogel V, Mantele W, Dotsch V EMBO J. 2007 Jul 25;26(14):3463-73. Epub 2007 Jun 21. PMID:17581633<ref>PMID:17581633</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2rp5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Doetsch V]] |
| - | [[Category: | + | [[Category: Ou HD]] |
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Current revision
Solution structure of the oligomerization domain in CEP-1
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