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PDBsum entry 2k1j
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protein metals links
Gene regulation PDB id
2k1j

 

 

 

 

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Contents
Protein chain
63 a.a. *
Metals
_ZN ×2
* Residue conservation analysis
PDB id:
2k1j
Name: Gene regulation
Title: Plan homeodomain finger of tumour supressor ing4
Structure: Inhibitor of growth protein 4. Chain: a. Fragment: phd-type zinc-finger, unp residues 188-249. Synonym: p29ing4. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ing4. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 25 models
Authors: A.Palacios,P.Garcia,D.Padro,E.Lopez-Hernandez,F.J.Blanco
Key ref: A.Palacios et al. (2006). Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4. Febs Lett, 580, 6903-6908. PubMed id: 17157298
Date:
05-Mar-08     Release date:   15-Apr-08    
Supersedes: 2jmq
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UNL4  (ING4_HUMAN) -  Inhibitor of growth protein 4 from Homo sapiens
Seq:
Struc: 		249 a.a.
63 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Febs Lett 580:6903-6908 (2006)
PubMed id: 17157298  
 
 
Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.
A.Palacios, P.Garcia, D.Padró, E.López-Hernández, I.Martín, F.J.Blanco.
 
  ABSTRACT  
 
Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20803232 A.H.Aguissa-Touré, R.P.Wong, and G.Li (2011).
The ING family tumor suppressors: from structure to function.
  Cell Mol Life Sci, 68, 45-54.  
21078114 M.Abad, A.Moreno, A.Palacios, M.Narita, F.Blanco, G.Moreno-Bueno, M.Narita, and I.Palmero (2011).
The tumor suppressor ING1 contributes to epigenetic control of cellular senescence.
  Aging Cell, 10, 158-171.  
21052543 X.Li, K.Kikuchi, and Y.Takano (2011).
ING Genes Work as Tumor Suppressor Genes in the Carcinogenesis of Head and Neck Squamous Cell Carcinoma.
  J Oncol, 2011, 963614.  
20705953 A.Moreno, A.Palacios, J.L.Orgaz, B.Jimenez, F.J.Blanco, and I.Palmero (2010).
Functional impact of cancer-associated mutations in the tumor suppressor protein ING4.
  Carcinogenesis, 31, 1932-1938.
PDB code: 2m1r
20923397 K.L.Yap, and M.M.Zhou (2010).
Keeping it in the family: diverse histone recognition by conserved structural folds.
  Crit Rev Biochem Mol Biol, 45, 488-505.  
19302042 D.Mathis, and C.Benoist (2009).
Aire.
  Annu Rev Immunol, 27, 287-312.  
19015549 J.Luo, S.Shah, K.Riabowol, and P.E.Mains (2009).
The Caenorhabditis elegans ing-3 gene regulates ionizing radiation-induced germ-cell apoptosis in a p53-associated pathway.
  Genetics, 181, 473-482.  
19442115 K.S.Champagne, and T.G.Kutateladze (2009).
Structural insight into histone recognition by the ING PHD fingers.
  Curr Drug Targets, 10, 432-441.  
19432890 M.Unoki, K.Kumamoto, S.Takenoshita, and C.C.Harris (2009).
Reviewing the current classification of inhibitor of growth family proteins.
  Cancer Sci, 100, 1173-1179.  
19187765 T.Hung, O.Binda, K.S.Champagne, A.J.Kuo, K.Johnson, H.Y.Chang, M.D.Simon, T.G.Kutateladze, and O.Gozani (2009).
ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation.
  Mol Cell, 33, 248-256.
PDB code: 2pnx
18381289 A.Palacios, I.G.Muñoz, D.Pantoja-Uceda, M.J.Marcaida, D.Torres, J.M.Martín-García, I.Luque, G.Montoya, and F.J.Blanco (2008).
Molecular basis of histone H3K4me3 recognition by ING4.
  J Biol Chem, 283, 15956-15964.
PDB code: 2vnf
18691180 M.A.Soliman, P.Berardi, S.Pastyryeva, P.Bonnefin, X.Feng, A.Colina, D.Young, and K.Riabowol (2008).
ING1a expression increases during replicative senescence and induces a senescent phenotype.
  Aging Cell, 7, 783-794.  
18794358 M.Ullah, N.Pelletier, L.Xiao, S.P.Zhao, K.Wang, C.Degerny, S.Tahmasebi, C.Cayrou, Y.Doyon, S.L.Goh, N.Champagne, J.Côté, and X.J.Yang (2008).
Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes.
  Mol Cell Biol, 28, 6828-6843.  
18779315 S.Nozell, T.Laver, D.Moseley, L.Nowoslawski, M.De Vos, G.P.Atkinson, K.Harrison, L.B.Nabors, and E.N.Benveniste (2008).
The ING4 tumor suppressor attenuates NF-kappaB activity at the promoters of target genes.
  Mol Cell Biol, 28, 6632-6645.  
18836436 X.Han, X.Feng, J.B.Rattner, H.Smith, P.Bose, K.Suzuki, M.A.Soliman, M.S.Scott, B.E.Burke, and K.Riabowol (2008).
Tethering by lamin A stabilizes and targets the ING1 tumour suppressor.
  Nat Cell Biol, 10, 1333-1340.  
17949986 M.A.Soliman, and K.Riabowol (2007).
After a decade of study-ING, a PHD for a versatile family of proteins.
  Trends Biochem Sci, 32, 509-519.  
17693408 M.Abad, C.Menéndez, A.Füchtbauer, M.Serrano, E.M.Füchtbauer, and I.Palmero (2007).
Ing1 mediates p53 accumulation and chromatin modification in response to oncogenic stress.
  J Biol Chem, 282, 31060-31067.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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