1U9G
Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(8)L(9)
Summary for 1U9G
| Entry DOI | 10.2210/pdb1u9g/pdb |
| Related | 1U9F 1U9H |
| Descriptor | General control protein GCN4, SULFATE ION (3 entities in total) |
| Functional Keywords | tetrameric alpha-helical coiled coil with heteerocycic backbone modification, transcription |
| Total number of polymer chains | 2 |
| Total formula weight | 8093.45 |
| Authors | Horne, W.S.,Yadav, M.K.,Stout, C.D.,Ghadiri, M.R. (deposition date: 2004-08-09, release date: 2004-11-30, Last modification date: 2011-07-13) |
| Primary citation | Horne, W.S.,Yadav, M.K.,Stout, C.D.,Ghadiri, M.R. Heterocyclic peptide backbone modifications in an alpha-helical coiled coil. J.Am.Chem.Soc., 126:15366-15367, 2004 Cited by PubMed Abstract: 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. PubMed: 15563148DOI: 10.1021/ja0450408 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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