PDBsum entry 3o35

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Transcription/protein binding PDB id
Protein chain
178 a.a. *
_ZN ×4
Waters ×248
* Residue conservation analysis
PDB id:
Name: Transcription/protein binding
Title: Crystal structure of trim24 phd-bromo complexed with h3(23-3 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 h3.1. Chain: d, e. Fragment: unp residues 14 -22.
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
1.76Å     R-factor:   0.206     R-free:   0.225
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
23-Jul-10     Release date:   15-Dec-10    
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Protein chains
Pfam   ArchSchema ?
O15164  (TIF1A_HUMAN) -  Transcription intermediary factor 1-alpha
1050 a.a.
178 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 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.
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
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