2rp4
From Proteopedia
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| - | + | ==Solution Structure of the oligomerization domain in Dmp53== | |
| - | + | <StructureSection load='2rp4' size='340' side='right' caption='[[2rp4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | === | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2rp4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RP4 FirstGlance]. <br> | |
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rp5|2rp5]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p53, prac, CG10873, Dmel_CG33336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</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=2rp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rp4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rp4 RCSB], [http://www.ebi.ac.uk/pdbsum/2rp4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
| - | [[Category: Doetsch, V | + | [[Category: Doetsch, V]] |
| - | [[Category: Ou, H D | + | [[Category: Ou, H D]] |
[[Category: Dmp53]] | [[Category: Dmp53]] | ||
[[Category: Nucleus]] | [[Category: Nucleus]] | ||
Revision as of 14:17, 17 December 2014
Solution Structure of the oligomerization domain in Dmp53
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