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PDBsum entry 3he5
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protein Protein-protein interface(s) links
De novo protein PDB id
3he5

 

 

 

 

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Contents
Protein chains
47 a.a.
48 a.a.
Waters ×117
PDB id:
3he5
Name: De novo protein
Title: Heterospecific coiled-coil pair synzip2:synzip1
Structure: Synzip1. Chain: a, c, e. Engineered: yes. Synzip2. Chain: b, d, f. Engineered: yes
Source: Artificial gene. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.75Å     R-factor:   0.192     R-free:   0.228
Authors: A.W.Reinke,R.A.Grant,A.E.Keating
Key ref: A.W.Reinke et al. (2010). A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering. J Am Chem Soc, 132, 6025-6031. PubMed id: 20387835
Date:
07-May-09     Release date:   23-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 47 a.a.
Protein chains
No UniProt id for this chain
Struc: 48 a.a.
Key:    Secondary structure  CATH domain

 

 
J Am Chem Soc 132:6025-6031 (2010)
PubMed id: 20387835  
 
 
A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering.
A.W.Reinke, R.A.Grant, A.E.Keating.
 
  ABSTRACT  
 
The versatile coiled-coil protein motif is widely used to induce and control macromolecular interactions in biology and materials science. Yet the types of interaction patterns that can be constructed using known coiled coils are limited. Here we greatly expand the coiled-coil toolkit by measuring the complete pairwise interactions of 48 synthetic coiled coils and 7 human bZIP coiled coils using peptide microarrays. The resulting 55-member protein "interactome" includes 27 pairs of interacting peptides that preferentially heteroassociate. The 27 pairs can be used in combinations to assemble sets of 3 to 6 proteins that compose networks of varying topologies. Of special interest are heterospecific peptide pairs that participate in mutually orthogonal interactions. Such pairs provide the opportunity to dimerize two separate molecular systems without undesired crosstalk. Solution and structural characterization of two such sets of orthogonal heterodimers provide details of their interaction geometries. The orthogonal pair, along with the many other network motifs discovered in our screen, provide new capabilities for synthetic biology and other applications.
 

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.  
21199371 J.A.Worrall, and J.M.Mason (2011).
Thermodynamic analysis of Jun-Fos coiled coil peptide antagonists.
  FEBS J, 278, 663-672.  
21458342 J.Karanicolas, J.E.Corn, I.Chen, L.A.Joachimiak, O.Dym, S.H.Peck, S.Albeck, T.Unger, W.Hu, G.Liu, S.Delbecq, G.T.Montelione, C.P.Spiegel, D.R.Liu, and D.Baker (2011).
A de novo protein binding pair by computational design and directed evolution.
  Mol Cell, 42, 250-260.
PDB codes: 3q9n 3q9u 3qa9
21354428 T.S.Chen, A.W.Reinke, and A.E.Keating (2011).
Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1.
  J Mol Biol, 408, 304-320.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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