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. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|