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A potential molecular switch in an alpha-helical coiled coil.
Proteins. 2008 Jan 01; 70(1):25-30.P

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.

Authors+Show Affiliations

Laughton CA
School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom.
Luisi BF
No affiliation info available
Pratap JV
No affiliation info available
Calladine CR
No affiliation info available

MeSH

Allosteric RegulationBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription Factors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17654543

Citation

Laughton, Charles A., et al. "A Potential Molecular Switch in an Alpha-helical Coiled Coil." Proteins, vol. 70, no. 1, 2008, pp. 25-30.
Laughton CA, Luisi BF, Pratap JV, et al. A potential molecular switch in an alpha-helical coiled coil. Proteins. 2008;70(1):25-30.
Laughton, C. A., Luisi, B. F., Pratap, J. V., & Calladine, C. R. (2008). A potential molecular switch in an alpha-helical coiled coil. Proteins, 70(1), 25-30.
Laughton CA, et al. A Potential Molecular Switch in an Alpha-helical Coiled Coil. Proteins. 2008 Jan 1;70(1):25-30. PubMed PMID: 17654543.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A potential molecular switch in an alpha-helical coiled coil. AU - Laughton,Charles A, AU - Luisi,Ben F, AU - Pratap,J Venkatesh, AU - Calladine,Chris R, PY - 2007/7/27/pubmed PY - 2008/1/17/medline PY - 2007/7/27/entrez SP - 25 EP - 30 JF - Proteins JO - Proteins VL - 70 IS - 1 N2 - 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. SN - 1097-0134 UR - https://www.unboundmedicine.com/medline/citation/17654543/A_potential_molecular_switch_in_an_alpha_helical_coiled_coil_ L2 - https://doi.org/10.1002/prot.21596 DB - PRIME DP - Unbound Medicine ER -