2OVN

NMR structure of the GCN4 trigger peptide

2OVN の概要

• エントリーDOI: 10.2210/pdb2ovn/pdb
• 分子名称: General control protein GCN4 (1 entity in total)
• 機能のキーワード: gcn4, coiled-coil, trigger peptide, transcription
• 細胞内の位置: Nucleus: P03069
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2016.30

構造登録者

Matousek, W.M.,Alexandrescu, A.T. (登録日: 2007-02-14, 公開日: 2007-04-03, 最終更新日: 2024-05-22)

主引用文献

Steinmetz, M.O.,Jelesarov, I.,Matousek, W.M.,Honnappa, S.,Jahnke, W.,Missimer, J.H.,Frank, S.,Alexandrescu, A.T.,Kammerer, R.A.
Molecular basis of coiled-coil formation.
Proc.Natl.Acad.Sci.Usa, 104:7062-7067, 2007

PubMed Abstract: Coiled coils have attracted considerable interest as design templates in a wide range of applications. Successful coiled-coil design strategies therefore require a detailed understanding of coiled-coil folding. One common feature shared by coiled coils is the presence of a short autonomous helical folding unit, termed "trigger sequence," that is indispensable for folding. Detailed knowledge of trigger sequences at the molecular level is thus key to a general understanding of coiled-coil formation. Using a multidisciplinary approach, we identify and characterize here the molecular determinants that specify the helical conformation of the monomeric early folding intermediate of the GCN4 coiled coil. We demonstrate that a network of hydrogen-bonding and electrostatic interactions stabilize the trigger-sequence helix. This network is rearranged in the final dimeric coiled-coil structure, and its destabilization significantly slows down GCN4 leucine zipper folding. Our findings provide a general explanation for the molecular mechanism of coiled-coil formation.

PubMed: 17438295
DOI: 10.1073/pnas.0700321104

実験手法

SOLUTION NMR