2PNX

The PHD finger of ING4 in complex with an H3K4Me3 histone peptide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.199 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation

Hung, T.Binda, O.Champagne, K.S.Kuo, A.J.Johnson, K.Chang, H.Y.Simon, M.D.Kutateladze, T.G.Gozani, O.

(2009) Mol Cell 33: 248-256

  • DOI: https://doi.org/10.1016/j.molcel.2008.12.016
  • Primary Citation of Related Structures:  
    2PNX

  • PubMed Abstract: 

    Aberrations in chromatin dynamics play a fundamental role in tumorigenesis, yet relatively little is known of the molecular mechanisms linking histone lysine methylation to neoplastic disease. ING4 (Inhibitor of Growth 4) is a native subunit of an HBO1 histone acetyltransferase (HAT) complex and a tumor suppressor protein. Here we show a critical role for specific recognition of histone H3 trimethylated at lysine 4 (H3K4me3) by the ING4 PHD finger in mediating ING4 gene expression and tumor suppressor functions. The interaction between ING4 and H3K4me3 augments HBO1 acetylation activity on H3 tails and drives H3 acetylation at ING4 target promoters. Further, ING4 facilitates apoptosis in response to genotoxic stress and inhibits anchorage-independent cell growth, and these functions depend on ING4 interactions with H3K4me3. Together, our results demonstrate a mechanism for brokering crosstalk between H3K4 methylation and H3 acetylation and reveal a molecular link between chromatin modulation and tumor suppressor mechanisms.


  • Organizational Affiliation

    Department of Biology, Stanford University, Stanford, CA 94305, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Inhibitor of growth protein 4
A, C
55Homo sapiensMutation(s): 0 
Gene Names: ING4
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UNL4 (Homo sapiens)
Explore Q9UNL4 
Go to UniProtKB:  Q9UNL4
PHAROS:  Q9UNL4
GTEx:  ENSG00000111653 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UNL4
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
H3K4Me3 peptide
B, D
12N/AMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.199 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.16α = 90
b = 68.16β = 90
c = 27.96γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
SOLVEphasing
CNSrefinement
d*TREKdata reduction
d*TREKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-04-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance