ArticleStructure (London, England : 1993)2015
A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- NOD-Like Receptor Genes Undergo Diversity-Enhancing Evolution in a Fungal Species Complex.Genome biology and evolution · 2026Article
- Reconstructing NOD-like receptor alleles with high internal conservation inMicrobial genomics · 2025Article
- Discovery and Analysis of Repeat and Low-Complexity Architectures in Proteins and Their Conserved Evolutionary Relationships Using Self-Homology Dot Plots.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing.PLoS pathogens · 2022Article
- The Repeating, Modular Architecture of the HtrA Proteases.Biomolecules · 2022Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Analysis of Tandem Repeat Protein Folding Using Nearest-Neighbor Models.Annual review of biophysics · 2021Review
- A collection of programs for one-dimensional Ising analysis of linear repeat proteins with point substitutions.Protein science : a publication of the Protein Society · 2021Article
- The Effect of Mutations in the TPR and Ankyrin Families of Alpha Solenoid Repeat Proteins.Frontiers in bioinformatics · 2021Review
- Self-analysis of repeat proteins reveals evolutionarily conserved patterns.BMC bioinformatics · 2020Article
- The use of consensus sequence information to engineer stability and activity in proteins.Methods in enzymology · 2020Article
- Extreme stability in de novo-designed repeat arrays is determined by unusually stable short-range interactions.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain.PloS one · 2017Article
- Ssn6-Tup1 global transcriptional co-repressor: Role of the N-terminal glutamine-rich region of Ssn6.PloS one · 2017Article
- Broken TALEs: Transcription Activator-like Effectors Populate Partly Folded States.Biophysical journal · 2016Article
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4 authors.
Funding
Abstract
Linear repeat proteins often have high structural similarity and low (∼25%) pairwise sequence identities (PSI) among modules. We identified a unique P. anserina (Pa) sequence with tetratricopeptide repeat (TPR) homology, which contains longer (42 residue) repeats (42PRs) with an average PSI >91%. We determined the crystal structure of five tandem Pa 42PRs to 1.6 Å, and examined the stability and solution properties of constructs containing three to six Pa 42PRs. Compared with 34-residue TPRs (34PRs), Pa 42PRs have a one-turn extension of each helix, and bury more surface area. Unfolding transitions shift to higher denaturant concentration and become sharper as repeats are added. Fitted Ising models show Pa 42PRs to be more cooperative than consensus 34PRs, with increased magnitudes of intrinsic and interfacial free energies. These results demonstrate the tolerance of the TPR motif to length variation, and provide a basis to understand the effects of helix length on intrinsic/interfacial stability.
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