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PDBsum entry 1sbx

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protein links
Oncoprotein PDB id
1sbx
Jmol
Contents
Protein chain
106 a.a. *
Waters ×79
* Residue conservation analysis
PDB id:
1sbx
Name: Oncoprotein
Title: Crystal structure of the dachshund-homology domain of human ski
Structure: Ski oncogene. Chain: a. Fragment: dachshund-homology domain of human ski. Synonym: c-ski. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ski. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.65Å     R-factor:   0.170     R-free:   0.206
Authors: J.J.Wilson,M.Malakhova,R.Zhang,A.Joachimiak,R.S.Hegde
Key ref:
J.J.Wilson et al. (2004). Crystal structure of the dachshund homology domain of human SKI. Structure, 12, 785-792. PubMed id: 15130471 DOI: 10.1016/j.str.2004.02.035
Date:
11-Feb-04     Release date:   25-May-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P12755  (SKI_HUMAN) -  Ski oncogene
Seq:
Struc:
 
Seq:
Struc:
728 a.a.
106 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     transcription, DNA-dependent   1 term 

 

 
DOI no: 10.1016/j.str.2004.02.035 Structure 12:785-792 (2004)
PubMed id: 15130471  
 
 
Crystal structure of the dachshund homology domain of human SKI.
J.J.Wilson, M.Malakhova, R.Zhang, A.Joachimiak, R.S.Hegde.
 
  ABSTRACT  
 
The nuclear protooncoprotein SKI negatively regulates transforming growth factor-beta (TGF-beta) signaling in cell growth and differentiation. It directly interacts with the Smads and, by various mechanisms, represses the transcription of TGF-beta-responsive genes. SKI is a multidomain protein that includes a domain bearing high sequence similarity with the retinal determination protein Dachshund (the Dachshund homology domain, DHD). The SKI-DHD has been implicated in SMAD-2/3, N-CoR, SKIP, and PML-RARalpha binding. The 1.65 A crystal structure of the Dachshund homology domain of human SKI is reported here. The SKI-DHD adopts a mixed alpha/beta structure which includes features found in the forkhead/winged-helix family of DNA binding proteins, although SKI-DHD is not a DNA binding domain. Residues that form a contiguous surface patch on SKI-DHD are conserved within the Ski/Sno family and with Dachshund, suggesting that this domain may mediate intermolecular interactions common to these proteins.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Structure of the SKI Dachshund Homology Domain(A) Stereoview of an omit map contoured at 1.5s. The region of protein around Phe169 is in the loop between aC and b5. Figure generated using POVScript (Fenn et al., 2003).(B) Topology of SKI-DHD. Helices are shown as red cylinders, and strands are indicated by blue arrows.(C) Structure of SKI-DHD. Helices are in cyan and strands in green. Residues in the 3[10] helix (shown in blue) at the N terminus arise as a result of the cloning process. Figure generated by the program RIBBONS (Carson, 1987).
 
  The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 785-792) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23023332 A.J.Doyle, J.J.Doyle, S.L.Bessling, S.Maragh, M.E.Lindsay, D.Schepers, E.Gillis, G.Mortier, T.Homfray, K.Sauls, R.A.Norris, N.D.Huso, D.Leahy, D.W.Mohr, M.J.Caulfield, A.F.Scott, A.Destrée, R.C.Hennekam, P.H.Arn, C.J.Curry, L.Van Laer, A.S.McCallion, B.L.Loeys, and H.C.Dietz (2012).
Mutations in the TGF-β repressor SKI cause Shprintzen-Goldberg syndrome with aortic aneurysm.
  Nat Genet, 44, 1249-1254.  
20957027 T.Nyman, L.Trésaugues, M.Welin, L.Lehtiö, S.Flodin, C.Persson, I.Johansson, M.Hammarström, and P.Nordlund (2010).
The crystal structure of the Dachshund domain of human SnoN reveals flexibility in the putative protein interaction surface.
  PLoS One, 5, e12907.  
19008232 H.Zhang, and E.Stavnezer (2009).
Ski regulates muscle terminal differentiation by transcriptional activation of myog in a complex with six1 and eya3.
  J Biol Chem, 284, 2867-2879.  
19114989 J.Deheuninck, and K.Luo (2009).
Ski and SnoN, potent negative regulators of TGF-beta signaling.
  Cell Res, 19, 47-57.  
19383336 M.Nanjundan, K.W.Cheng, F.Zhang, J.Lahad, W.L.Kuo, R.Schmandt, K.Smith-McCune, D.Fishman, J.W.Gray, and G.B.Mills (2008).
Overexpression of SnoN/SkiL, amplified at the 3q26.2 locus, in ovarian cancers: a role in ovarian pathogenesis.
  Mol Oncol, 2, 164-181.  
16966324 Y.H.Hsu, K.P.Sarker, I.Pot, A.Chan, S.J.Netherton, and S.Bonni (2006).
Sumoylated SnoN represses transcription in a promoter-specific manner.
  J Biol Chem, 281, 33008-33018.  
15986136 J.A.Reed, Q.Lin, D.Chen, I.S.Mian, and E.E.Medrano (2005).
SKI pathways inducing progression of human melanoma.
  Cancer Metastasis Rev, 24, 265-272.  
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.