ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- Notch ankyrin domain: evolutionary rise of a thermodynamic sensor.Cell communication and signaling : CCS · 2022Article
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 2022Article
- Resolving the fine structure in the energy landscapes of repeat proteins.QRB discovery · 2022Article
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- Review
- Testing the length limit of loop grafting in a helical repeat protein.Current research in structural biology · 2021Article
- Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Phosphorylation-induced unfolding regulates p19Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins.Biophysical journal · 2018Article
- Diffuse transition state structure for the unfolding of a leucine-rich repeat protein.Physical chemistry chemical physics : PCCP · 2014Article
- Dissecting the critical factors for thermodynamic stability of modular proteins using molecular modeling approach.PloS one · 2014Article
- A disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBα.PLoS computational biology · 2013Article
- Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Biophysical journal · 2012Article
- Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.Protein science : a publication of the Protein Society · 2012Article
- Folding kinetics of the cooperatively folded subdomain of the IκBα ankyrin repeat domain.Journal of molecular biology · 2011Article
- Mechanical unfolding of an ankyrin repeat protein.Biophysical journal · 2010Article
- Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Repeat proteins are widespread in nature, with many of them functioning as binding molecules in protein-protein recognition. Their simple structural architecture is used in biotechnology for generating proteins with high affinities to target proteins. Recent folding studies of ankyrin repeat (AR) proteins revealed a new mechanism of protein folding. The formation of an intermediate state is rate limiting in the folding reaction, suggesting a scaffold function of this transient state for intrinsically less stable ARs. To investigate a possible common mechanism of AR folding, we studied the structure and folding of a new thermophilic AR protein (tANK) identified in the archaeon Thermoplasma volcanium. The x-ray structure of the evolutionary much older tANK revealed high homology to the human CDK inhibitor p19(INK4d), whose sequence was used for homology search. As for p19(INK4d), equilibrium and kinetic folding analyses classify tANK to the family of sequential three-state folding proteins, with an unusual fast equilibrium between native and intermediate state. Under equilibrium conditions, the intermediate can be populated to >90%, allowing characterization on a residue-by-residue level using NMR spectroscopy. These data clearly show that the three C-terminal ARs are natively folded in the intermediate state, whereas native cross-peaks for the rest of the molecule are missing. Therefore, the formation of a stable folding unit consisting of three ARs is the necessary rate-limiting step before AR 1 and 2 can assemble to form the native state.
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