ArticleProceedings of the National Academy of Sciences of the United States of America2015
Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Variants in CFAP410 cause a range of retinal and skeletal phenotypes.NPJ genomic medicine · 2025Article
- Equine ANP32 proteins support influenza A virus RNA polymerase activity.Virologica Sinica · 2023Article
- High Pressure CPMG and CEST Reveal That Cavity Position Dictates Distinct Dynamic Disorder in the PP32 Repeat Protein.The journal of physical chemistry. B · 2022Article
- Inline small-angle X-ray scattering-coupled chromatography under extreme hydrostatic pressure.Protein science : a publication of the Protein Society · 2022Article
- Designed leucine-rich repeat proteins bind two muramyl dipeptide ligands.Protein science : a publication of the Protein Society · 2021Article
- A Second Backbone: The Contribution of a Buried Asparagine Ladder to the Global and Local Stability of a Leucine-Rich Repeat Protein.Biochemistry · 2019Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- The consequences of cavity creation on the folding landscape of a repeat protein depend upon context.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- The case for defined protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Inferring repeat-protein energetics from evolutionary information.PLoS computational biology · 2017Article
- High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.Biophysical journal · 2016Article
- Detailing Protein Landscapes under Pressure.Biophysical journal · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
The leucine-rich repeat domain of PP32 is composed of five β-strand-containing repeats anchored by terminal caps. These repeats differ in sequence but are similar in structure, providing a means to connect topology, sequence, and folding pathway selection. Through kinetic studies of PP32, we find folding to be rate-limited by the formation of an on-pathway intermediate. Destabilizing core substitutions reveal a transition state ensemble that is highly polarized toward the C-terminal repeat and cap. To determine if this nucleus for folding corresponds to the most stable region of PP32, we monitored amide hydrogen exchange by NMR spectroscopy. Indeed, we find the highest protection to be biased toward the C terminus. Sequence manipulations that destabilize the C terminus spread out the transition state toward the middle of the protein. Consistent with results for helical ankyrin repeat proteins, these results suggest that local stabilities determine folding pathways.
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