1U9F

Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of K(15)L(16)

1U9F の概要

• エントリーDOI: 10.2210/pdb1u9f/pdb
• 関連するPDBエントリー: 1U9G 1U9H
• 分子名称: General control protein GCN4 (2 entities in total)
• 機能のキーワード: tetrameric alpha-helical coiled coil, heterocycic backbone modification, transcription
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 16098.94

構造登録者

Horne, W.S.,Yadav, M.K.,Stout, C.D.,Ghadiri, M.R. (登録日: 2004-08-09, 公開日: 2004-11-30, 最終更新日: 2011-07-13)

主引用文献

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

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: 15563148
DOI: 10.1021/ja0450408

実験手法

X-RAY DIFFRACTION (2.2 Å)