A potential molecular switch in an alpha-helical coiled coil
Related Experiment Video
Updated: Jul 13, 2026

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
Published on: March 1, 2022
Charles A Laughton1, Ben F Luisi, J Venkatesh Pratap
1School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom.
Abstract:
The yeast DNA-binding protein GCN4 forms a homo-dimer through a self-complementary coiled-coil interface. In this article, we describe how such coiled-coils might be bistable and, through Molecular Dynamics computations on the GCN4 coiled coil, we show that the coiled coil can indeed switch between the two states by a pathway in which there is a progressive "flipping" of consecutive steps along the interface. We discuss the general implications of potentially bistable coiled-coil interfaces for allosteric signal-transmission mechanisms along homo-dimeric coiled coils and for the packing of helices in globular proteins.
More Related Videos
13:02Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
07:08Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions