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PDBsum entry 3o36

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protein ligands metals Protein-protein interface(s) links
Transcription/protein binding PDB id
3o36
Jmol
Contents
Protein chain
184 a.a. *
Ligands
ALY
GLY-ALA-ALY
Metals
_ZN ×4
Waters ×342
* Residue conservation analysis
PDB id:
3o36
Name: Transcription/protein binding
Title: Crystal structure of trim24 phd-bromo complexed with h4(14-1 peptide
Structure: Transcription intermediary factor 1-alpha. Chain: a, b. Fragment: unp residues 824-1006. Synonym: tif1-alpha, tripartite motif-containing protein 24 finger protein 82. Engineered: yes. Histone h4. Chain: d, e. Fragment: unp residues 15-20.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: trim24, rnf82, tif1, tif1a. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence occurs naturally in humans
Resolution:
1.70Å     R-factor:   0.191     R-free:   0.216
Authors: Z.Wang,D.J.Patel
Key ref: W.W.Tsai et al. (2010). TRIM24 links a non-canonical histone signature to breast cancer. Nature, 468, 927-932. PubMed id: 21164480
Date:
23-Jul-10     Release date:   15-Dec-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O15164  (TIF1A_HUMAN) -  Transcription intermediary factor 1-alpha
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1050 a.a.
184 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     zinc ion binding     1 term  

 

 
Nature 468:927-932 (2010)
PubMed id: 21164480  
 
 
TRIM24 links a non-canonical histone signature to breast cancer.
W.W.Tsai, Z.Wang, T.T.Yiu, K.C.Akdemir, W.Xia, S.Winter, C.Y.Tsai, X.Shi, D.Schwarzer, W.Plunkett, B.Aronow, O.Gozani, W.Fischle, M.C.Hung, D.J.Patel, M.C.Barton.
 
  ABSTRACT  
 
Recognition of modified histone species by distinct structural domains within 'reader' proteins plays a critical role in the regulation of gene expression. Readers that simultaneously recognize histones with multiple marks allow transduction of complex chromatin modification patterns into specific biological outcomes. Here we report that chromatin regulator tripartite motif-containing 24 (TRIM24) functions in humans as a reader of dual histone marks by means of tandem plant homeodomain (PHD) and bromodomain (Bromo) regions. The three-dimensional structure of the PHD-Bromo region of TRIM24 revealed a single functional unit for combinatorial recognition of unmodified H3K4 (that is, histone H3 unmodified at lysine 4, H3K4me0) and acetylated H3K23 (histone H3 acetylated at lysine 23, H3K23ac) within the same histone tail. TRIM24 binds chromatin and oestrogen receptor to activate oestrogen-dependent genes associated with cellular proliferation and tumour development. Aberrant expression of TRIM24 negatively correlates with survival of breast cancer patients. The PHD-Bromo of TRIM24 provides a structural rationale for chromatin activation through a non-canonical histone signature, establishing a new route by which chromatin readers may influence cancer pathogenesis.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23211769 C.A.Musselman, M.E.Lalonde, J.Côté, and T.G.Kutateladze (2012).
Perceiving the epigenetic landscape through histone readers.
  Nat Struct Mol Biol, 19, 1218-1227.  
22473383 E.L.Greer, and Y.Shi (2012).
Histone methylation: a dynamic mark in health, disease and inheritance.
  Nat Rev Genet, 13, 343-357.  
21272588 K.E.Gardner, C.D.Allis, and B.D.Strahl (2011).
OPERating ON Chromatin, a Colorful Language where Context Matters.
  J Mol Biol, 409, 36-46.  
21666677 S.Eustermann, J.C.Yang, M.J.Law, R.Amos, L.M.Chapman, C.Jelinska, D.Garrick, D.Clynes, R.J.Gibbons, D.Rhodes, D.R.Higgs, and D.Neuhaus (2011).
Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin.
  Nat Struct Mol Biol, 18, 777-782.
PDB code: 2lbm
21979307 S.Hatakeyama (2011).
TRIM proteins and cancer.
  Nat Rev Cancer, 11, 792-804.  
21666679 S.Iwase, B.Xiang, S.Ghosh, T.Ren, P.W.Lewis, J.C.Cochrane, C.D.Allis, D.J.Picketts, D.J.Patel, H.Li, and Y.Shi (2011).
ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.
  Nat Struct Mol Biol, 18, 769-776.
PDB codes: 3ql9 3qla 3qlc 3qln
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.