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==DAXX helical bundle (DHB) domain / Rassf1C complex== | |||
===DAXX | <StructureSection load='2kzu' size='340' side='right' caption='[[2kzu]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kzu]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KZU FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kzs|2kzs]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAXX, DADB-159G18.9-007, DAMC-227D19.15-007, DAQB-126H3.2-007, XXbac-BCX165D10.3-007, XXbac-BPG185D15.6-007 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RASSF1, hCG_17462 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2kzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kzu RCSB], [http://www.ebi.ac.uk/pdbsum/2kzu PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Death-associated protein|Death-associated protein]] | *[[Death-associated protein|Death-associated protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Escobar-Cabrera, E | [[Category: Escobar-Cabrera, E]] | ||
[[Category: Giovinazzi, S | [[Category: Giovinazzi, S]] | ||
[[Category: Ishov, A M | [[Category: Ishov, A M]] | ||
[[Category: Lau, D K.W | [[Category: Lau, D K.W]] | ||
[[Category: McIntosh, L P | [[Category: McIntosh, L P]] | ||
[[Category: Apoptosis]] | [[Category: Apoptosis]] | ||
[[Category: Daxx helical bundle domain]] | [[Category: Daxx helical bundle domain]] | ||
Revision as of 17:10, 17 December 2014
DAXX helical bundle (DHB) domain / Rassf1C complexDAXX helical bundle (DHB) domain / Rassf1C complex
Structural highlights
Publication Abstract from PubMedDAXX 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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