ArticleProtein science : a publication of the Protein Society1996
Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed.
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Sequence-Dependent Interaction of the Human Papillomavirus E2 Protein with the DNA Elements on Its DNA Replication Origin.International journal of molecular sciences · 2023Article
- Biophysical characterization of SARAH domain-mediated multimerization of Hippo pathway complexes inThe Journal of biological chemistry · 2020Article
- Structural and Functional Properties of the Capsid Protein of Dengue and RelatedInternational journal of molecular sciences · 2019Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Hepatitis E virus capsid protein assembles in 4M urea in the presence of salts.Protein science : a publication of the Protein Society · 2013Article
- Design and characterization of an enhanced repressor of human papillomavirus E2 protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Temperature and Mg2+ sensing by a novel PhoP-PhoQ two-component system for regulation of virulence in Edwardsiella tarda.The Journal of biological chemistry · 2010Article
- Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.Biochemistry · 2010Article
- Experimental snapshots of a protein-DNA binding landscape.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A decision tree model for the prediction of homodimer folding mechanism.Bioinformation · 2009Article
- Evolutionary and biophysical relationships among the papillomavirus E2 proteins.Frontiers in bioscience (Landmark edition) · 2009Review
- Comprehensive comparison of the interaction of the E2 master regulator with its cognate target DNA sites in 73 human papillomavirus types by sequence statistics.Nucleic acids research · 2008Article
- A quasi-spontaneous amyloid route in a DNA binding gene regulatory domain: The papillomavirus HPV16 E2 protein.Protein science : a publication of the Protein Society · 2007Article
- Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.Protein science : a publication of the Protein Society · 2007Article
- Biophysical characterization of the enzyme I of the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system.Biophysical journal · 2006Article
- Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers.Bioinformation · 2005Article
- The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.The Biochemical journal · 2003Article
- DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Folding of a dimeric beta-barrel: residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain.Protein science : a publication of the Protein Society · 2000Article
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Abstract
The equilibrium unfolding reaction of the C-terminal 80-amino-acid dimeric DNA-binding domain of human papillomavirus (HPV) strain 16 E2 protein has been investigated using fluorescence, far-UV CD, and equilibrium sedimentation. The stability of the HPV-16 E2 DNA-binding domain is concentration-dependent, and the unfolding reaction is well described as a two-state transition from folded dimer to unfolded monomer. The conformational stability of the protein, delta GH2O, was found to be 9.8 kcal/mol at pH 5.6, with the corresponding equilibrium unfolding/dissociation constant, Ku, being 6.5 x 10(-8) M. Equilibrium sedimentation experiments give a Kd of 3.0 x 10(-8) M, showing an excellent agreement between the two different techniques. Denaturation by temperature followed by the change in ellipticity also shows a concomitant disappearance of secondary and tertiary structures. The Ku changes dramatically at physiologically relevant pH's: with a change in pH from 6.1 to 7.0, it goes from 5.5 x 10(-8) M to 4.4 x 10(10) M. Our results suggest that, at the very low concentration of protein where DNA binding is normally measured (e.g., 10(-11) M), the protein is predominantly monomeric and unfolded. They also stress the importance of the coupling between folding and DNA binding.
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