Laughton CA, et al. (2008) A potential molecular switch in an alpha-helical coiled coil. Proteins 70(1):25-30
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. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
|Status: Published||Type: Journal Article||PubMed ID: 17654543|
Topics addressed in this paper
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|Protein Sequence Features|
|Protein/Nucleic Acid Structure|