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PDBsum entry 6f08

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protein ligands Protein-protein interface(s) links
Peptide binding protein PDB id
6f08

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
225 a.a.
Ligands
ARG-ARG-PRO-GLU-
SEP-ALA-PRO-ALA-
GLU
ARG-ARG-ARG-PRO-
GLU-SEP-ALA-PRO-
ALA-GLU
ARG-ARG-PRO-GLU-
SEP-ALA-PRO-ALA
ARG-ARG-PRO-GLU-
SEP-ALA-PRO-ALA-
GLU-SER
1PE
Waters ×693
PDB id:
6f08
Name: Peptide binding protein
Title: 14-3-3 zeta in complex with the human son of sevenless homolog 1 (sos1)
Structure: 14-3-3 protein zeta/delta. Chain: a, b, i, j. Synonym: protein kinasE C inhibitor protein 1,kcip-1. Engineered: yes. Son of sevenless homolog 1. Chain: d, k, n, q. Synonym: sos-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ywhaz. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
Resolution:
1.90Å     R-factor:   0.213     R-free:   0.267
Authors: A.Ballone,F.Centorrino,C.Ottmann,S.Guo,S.Leysen
Key ref: A.Ballone et al. (2018). Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1). J Struct Biol, 202, 210-215. PubMed id: 29408703 DOI: 10.1016/j.jsb.2018.01.011
Date:
17-Nov-17     Release date:   14-Feb-18    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P63104  (1433Z_HUMAN) -  14-3-3 protein zeta/delta from Homo sapiens
Seq:
Struc:
245 a.a.
225 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/j.jsb.2018.01.011 J Struct Biol 202:210-215 (2018)
PubMed id: 29408703  
 
 
Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1).
A.Ballone, F.Centorrino, M.Wolter, C.Ottmann.
 
  ABSTRACT  
 
The deviant Ras activation machinery is found in approximately 30% of all human cancers. SOS1 is an important protagonist of this pathway that plays a key-role in aberrant cell proliferation and differentiation. Interaction of SOS1 with 14-3-3 proteins modulates SOS1 activity in Ras-MAPK signaling. In the present study, we analyze the 14-3-3/SOS1 protein-protein interaction (PPI) by different biochemical assays and report the high resolution crystal structure of a 13-mer motif of SOS1 bound to 14-3-3ζ. These structural and functional insights are important for the evaluation of this PPI interface for small-molecule stabilization as a new starting point for modulating the Ras-Raf-MAPK pathway.
 

 

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