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PDBsum entry 3lw1

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protein ligands metals links
Peptide binding protein PDB id
3lw1
Jmol
Contents
Protein chain
235 a.a. *
Ligands
PHE-LYS-TPO-GLU-
GLY-PRO-ASP
GOL
Metals
_MG ×3
_CL
Waters ×404
* Residue conservation analysis
PDB id:
3lw1
Name: Peptide binding protein
Title: Binary complex of 14-3-3 sigma and p53 pt387-peptide
Structure: 14-3-3 protein sigma. Chain: a. Synonym: stratifin, epithelial cell marker protein 1. Engineered: yes. Peptide of cellular tumor antigen p53. Chain: p. Fragment: unp residues 385-393. Synonym: tumor suppressor p53, phosphoprotein p53, antigen ny-co-13.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hme1, sfn. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetic peptide, the full length protein p53 occurs in homo sapiens
Resolution:
1.28Å     R-factor:   0.128     R-free:   0.151
Authors: B.Schumacher,J.Mondry,P.Thiel,M.Weyand,C.Ottmann
Key ref: B.Schumacher et al. (2010). Structure of the p53 C-terminus bound to 14-3-3: implications for stabilization of the p53 tetramer. FEBS Lett, 584, 1443-1448. PubMed id: 20206173 DOI: 10.1016/j.febslet.2010.02.065
Date:
23-Feb-10     Release date:   23-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31947  (1433S_HUMAN) -  14-3-3 protein sigma
Seq:
Struc:
248 a.a.
235 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   7 terms 
  Biological process     keratinocyte development   22 terms 
  Biochemical function     protein binding     5 terms  

 

 
DOI no: 10.1016/j.febslet.2010.02.065 FEBS Lett 584:1443-1448 (2010)
PubMed id: 20206173  
 
 
Structure of the p53 C-terminus bound to 14-3-3: implications for stabilization of the p53 tetramer.
B.Schumacher, J.Mondry, P.Thiel, M.Weyand, C.Ottmann.
 
  ABSTRACT  
 
The adaptor protein 14-3-3 binds to and stabilizes the tumor suppressor p53 and enhances its anti-tumour activity. In the regulatory C-terminal domain of p53 several 14-3-3 binding motifs have been identified. Here, we report the crystal structure of the extreme C-terminus (residues 385-393, p53pT387) of p53 in complex with 14-3-3sigma at a resolution of 1.28A. p53pT387 is accommodated by 14-3-3 in a yet unrecognized fashion implying a rationale for 14-3-3 binding to the active p53 tetramer. The structure exhibits a potential binding site for small molecules that could stabilize the p53/14-3-3 protein complex suggesting the possibility for therapeutic intervention.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21071205 G.Schreiber, and A.E.Keating (2011).
Protein binding specificity versus promiscuity.
  Curr Opin Struct Biol, 21, 50-61.  
20839267 M.Kaiser, and C.Ottmann (2010).
The first small-molecule inhibitor of 14-3-3s: modulating the master regulator.
  Chembiochem, 11, 2085-2087.  
20487521 M.Zurita, P.C.Lara, R.del Moral, B.Torres, J.L.Linares-Fernández, S.R.Arrabal, J.Martínez-Galán, F.J.Oliver, and J.M.Ruiz de Almodóvar (2010).
Hypermethylated 14-3-3-sigma and ESR1 gene promoters in serum as candidate biomarkers for the diagnosis and treatment efficacy of breast cancer metastasis.
  BMC Cancer, 10, 217.  
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.