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PDBsum entry 2ko0

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protein dna_rna metals links
Transcription/DNA PDB id
2ko0

 

 

 

 

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Contents
Protein chain
87 a.a. *
DNA/RNA
Metals
_ZN
* Residue conservation analysis
PDB id:
2ko0
Name: Transcription/DNA
Title: Solution structure of the thap zinc finger of thap1 in complex with its DNA target
Structure: Thap domain-containing protein 1. Chain: a. Fragment: unp residues 1-82. Engineered: yes. Mutation: yes. Rrm1. Chain: b. Engineered: yes. Other_details: specific thap1 binding sequence element found in the
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: thap1. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3. Synthetic: yes. Other_details: DNA synthesis.
NMR struc: 15 models
Authors: S.Campagne,V.Gervais,O.Saurel,A.Milon
Key ref: S.Campagne et al. (2010). Structural determinants of specific DNA-recognition by the THAP zinc finger. Nucleic Acids Res, 38, 3466-3476. PubMed id: 20144952
Date:
08-Sep-09     Release date:   19-Jan-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9NVV9  (THAP1_HUMAN) -  THAP domain-containing protein 1 from Homo sapiens
Seq:
Struc:
213 a.a.
87 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DNA/RNA chains
  G-C-T-T-G-T-G-T-G-G-G-C-A-G-C-G 16 bases
  C-G-C-T-G-C-C-C-A-C-A-C-A-A-G-C 16 bases

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

 

 
Nucleic Acids Res 38:3466-3476 (2010)
PubMed id: 20144952  
 
 
Structural determinants of specific DNA-recognition by the THAP zinc finger.
S.Campagne, O.Saurel, V.Gervais, A.Milon.
 
  ABSTRACT  
 
Human THAP1 is the prototype of a large family of cellular factors sharing an original THAP zinc-finger motif responsible for DNA binding. Human THAP1 regulates endothelial cell proliferation and G1/S cell-cycle progression, through modulation of pRb/E2F cell-cycle target genes including rrm1. Recently, mutations in THAP1 have been found to cause DYT6 primary torsion dystonia, a human neurological disease. We report here the first 3D structure of the complex formed by the DNA-binding domain of THAP1 and its specific DNA target (THABS) found within the rrm1 target gene. The THAP zinc finger uses its double-stranded beta-sheet to fill the DNA major groove and provides a unique combination of contacts from the beta-sheet, the N-terminal tail and surrounding loops toward the five invariant base pairs of the THABS sequence. Our studies reveal unprecedented insights into the specific DNA recognition mechanisms within this large family of proteins controlling cell proliferation, cell cycle and pluripotency.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21134457 D.C.Bragg, I.A.Armata, F.C.Nery, X.O.Breakefield, and N.Sharma (2011).
Molecular pathways in dystonia.
  Neurobiol Dis, 42, 136-147.  
21168499 L.J.Ozelius, and S.B.Bressman (2011).
Genetic and clinical features of primary torsion dystonia.
  Neurobiol Dis, 42, 127-135.  
20976771 F.J.Kaiser, A.Osmanoric, A.Rakovic, A.Erogullari, N.Uflacker, D.Braunholz, T.Lohnau, S.Orolicki, M.Albrecht, G.Gillessen-Kaesbach, C.Klein, and K.Lohmann (2010).
The dystonia gene DYT1 is repressed by the transcription factor THAP1 (DYT6).
  Ann Neurol, 68, 554-559.  
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.

 

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