2KZS

DAXX helical bundle (DHB) domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 120 
  • Conformers Submitted: 25 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Characterization of the DAXX N-Terminal Helical Bundle Domain and Its Complex with Rassf1C.

Escobar-Cabrera, E.Lau, D.K.Giovinazzi, S.Ishov, A.M.McIntosh, L.P.

(2010) Structure 18: 1642-1653

  • DOI: https://doi.org/10.1016/j.str.2010.09.016
  • Primary Citation of Related Structures:  
    2KZS, 2KZU

  • PubMed Abstract: 

    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 α helix upon binding this DAXX domain via a shallow cleft along the flexible helices H2 and H5 (K(D) ∼60 μM). 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.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC V6T1Z3, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Death-associated protein 694Homo sapiensMutation(s): 0 
Gene Names: DAXXDADB-159G18.9-007DAMC-227D19.15-007DAQB-126H3.2-007XXbac-BCX165D10.3-007XXbac-BPG185D15.6-007
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UER7 (Homo sapiens)
Explore Q9UER7 
Go to UniProtKB:  Q9UER7
PHAROS:  Q9UER7
GTEx:  ENSG00000204209 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UER7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 120 
  • Conformers Submitted: 25 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-12-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2020-02-05
    Changes: Database references, Other
  • Version 1.3: 2023-06-14
    Changes: Database references, Other