1U9G: Heterocyclic Peptide Backbone Modification In Gcn4-Pli Based Coiled Coils: Replacement Of K(8)l(9)

In this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the alpha-helix as well as template an interhelical crossing between chains in the bundle.
PDB ID: 1U9GDownload
MMDB ID: 51632
PDB Deposition Date: 2004/8/9
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Similar Structures:
Biological Unit for 1U9G: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1U9G
Label Count Molecule
Proteins (4 molecules)
General Control Protein Gcn4
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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