ArticlePLoS computational biology2015
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family.
Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Deep phenotyping of EHMT1 ankyrin repeat domain missense variants in Kleefstra syndrome by multi-tiered structural genomics analyses at atomic resolution.Human molecular genetics · 2026Article
- A geometric criterion links HIV-1 capsid topography to its biophysical properties and function.Nature communications · 2026Article
- Enterocytes rely on purine biosynthesis/salvage pathway to facilitate dietary fat absorption.Nature communications · 2026Article
- Systematically identification of survival-associated eQTLs in a Japanese kidney cancer cohort.PLoS genetics · 2025Article
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Modeling ANKRD26 5'-UTR mutation-related thrombocytopenia.Disease models & mechanisms · 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
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- crANKing up the infection: ankyrin domains inInfection and immunity · 2024Review
- Transcriptome-wide Identification of Nine Tandem Repeat Protein Families in Roselle (Tropical life sciences research · 2024Article
- A contact-based analysis of local energetic frustration dynamics identifies key residues enabling RfaH fold-switch.Protein science : a publication of the Protein Society · 2024Article
- Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families.Nucleic acids research · 2024Article
- Evolution shapes interaction patterns for epistasis and specific protein binding in a two-component signaling system.Communications chemistry · 2024Article
- Local energetic frustration conservation in protein families and superfamilies.Nature communications · 2023Article
- Exploring the structural acrobatics of fold-switching proteins using simplified structure-based models.Biophysical reviews · 2023Review
- Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3.Cell reports · 2022Article
- Evolution and folding of repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Resolving the fine structure in the energy landscapes of repeat proteins.QRB discovery · 2022Article
- Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation.International journal of molecular sciences · 2021Review
- Comparative analysis of theOpen life sciences · 2021Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ankyrin repeat containing proteins are one of the most abundant solenoid folds. Usually implicated in specific protein-protein interactions, these proteins are readily amenable for design, with promising biotechnological and biomedical applications. Studying repeat protein families presents technical challenges due to the high sequence divergence among the repeating units. We developed and applied a systematic method to consistently identify and annotate the structural repetitions over the members of the complete Ankyrin Repeat Protein Family, with increased sensitivity over previous studies. We statistically characterized the number of repeats, the folding of the repeat-arrays, their structural variations, insertions and deletions. An energetic analysis of the local frustration patterns reveal the basic features underlying fold stability and its relation to the functional binding regions. We found a strong linear correlation between the conservation of the energetic features in the repeat arrays and their sequence variations, and discuss new insights into the organization and function of these ubiquitous proteins.
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