2kzu: Difference between revisions

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-{{Seed}}
-[[Image:2kzu.jpg|left|200px]]
-<!--
+==DAXX helical bundle (DHB) domain / Rassf1C complex==
-The line below this paragraph, containing "STRUCTURE_2kzu", creates the "Structure Box" on the page.
+<StructureSection load='2kzu' size='340' side='right'caption='[[2kzu]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2kzu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KZU FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=2kzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kzu OCA], [https://pdbe.org/2kzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kzu RCSB], [https://www.ebi.ac.uk/pdbsum/2kzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kzu ProSAT]</span></td></tr>
-{{STRUCTURE_2kzu|  PDB=2kzu  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DAXX_HUMAN DAXX_HUMAN] Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.<ref>PMID:12140263</ref> <ref>PMID:15364927</ref> <ref>PMID:17081986</ref> <ref>PMID:16845383</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+DAXX is a scaffold protein with diverse roles including transcription and cell cycle regulation. Using NMR spectroscopy, we demonstrate that the C-terminal half of DAXX is intrinsically disordered, whereas a folded domain is present near its N terminus. This domain forms a left-handed four-helix bundle (H1, H2, H4, H5). However, due to a crossover helix (H3), this topology differs from that of the Sin3 PAH domain, which to date has been used as a model for DAXX. The N-terminal residues of the tumor suppressor Rassf1C fold into an amphipathic alpha helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) approximately 60 muM). Based on a proposed DAXX recognition motif as hydrophobic residues preceded by negatively charged groups, we found that peptide models of p53 and Mdm2 also bound the helical bundle. These data provide a structural foundation for understanding the diverse functions of DAXX.
-===DAXX helical bundle (DHB) domain / Rassf1C complex===
+Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C.,Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP Structure. 2010 Dec 8;18(12):1642-53. PMID:21134643<ref>PMID:21134643</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2kzu" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21134643}}, adds the Publication Abstract to the page
+*[[Death-associated protein 3D structures|Death-associated protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21134643 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21134643}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KZU is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KZU OCA].
-==Reference==
-<ref group="xtra">PMID:21134643</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Escobar-Cabrera, E.]]
+[[Category: Large Structures]]
-[[Category: Giovinazzi, S.]]
+[[Category: Escobar-Cabrera E]]
-[[Category: Ishov, A M.]]
+[[Category: Giovinazzi S]]
-[[Category: Lau, D K.W.]]
+[[Category: Ishov AM]]
-[[Category: McIntosh, L P.]]
+[[Category: Lau DKW]]
-[[Category: Apoptosis]]
+[[Category: McIntosh LP]]
-[[Category: Daxx helical bundle domain]]
-[[Category: Fas death-domain associated protein]]
-[[Category: Ras-association domain family 1c protein]]
-[[Category: Tumor suppressor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:38:18 2010''