ArticleProtein science : a publication of the Protein Society2014
Capping motifs stabilize the leucine-rich repeat protein PP32 and rigidify adjacent repeats.
Article in Protein science : a publication of the Protein Society, 2014. 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.
- A (poly)Pro tip for preserving native disulfide connectivity during thiol-maleimide bioconjugation of disulfide-rich peptides.Chemical science · 2026Article
- 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
- Pathogenicity and functional analysis ofFrontiers in medicine · 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
- Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.Scientific reports · 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
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- CARMIL family proteins as multidomain regulators of actin-based motility.Molecular biology of the cell · 2017Article
- High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.Biophysical journal · 2016Article
- Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Computational design of a leucine-rich repeat protein with a predefined geometry.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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3 authors.
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Abstract
Capping motifs are found to flank most β-strand-containing repeat proteins. To better understand the roles of these capping motifs in organizing structure and stability, we carried out folding and solution NMR studies on the leucine-rich repeat (LRR) domain of PP32, which is composed of five tandem LRR, capped by α-helical and β-hairpin motifs on the N- and C-termini. We were able to purify PP32 constructs lacking either cap and containing destabilizing substitutions. Removing the C-cap results in complete unfolding of PP32. Removing the N-cap has a much less severe effect, decreasing stability but retaining much of its secondary structure. In contrast, the dynamics and tertiary structure of the first two repeats are significantly perturbed, based on (1)H-(15)N relaxation studies, chemical shift perturbations, and residual dipolar couplings. However, more distal repeats (3 to C-cap) retain their native tertiary structure. In this regard, the N-cap drives the folding of adjacent repeats from what appears to be a molten-globule-like state. This interpretation is supported by extensive analysis using core packing substitutions in the full-length and N-cap-truncated PP32. This work highlights the importance of caps to the stability and structural integrity of β-strand-containing LRR proteins, and emphasizes the different contributions of the N- and C-terminal caps.
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