ArticleNature structural & molecular biology2015
Control of repeat-protein curvature by computational protein design.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- HURDLER: a cloning method to overcome length limits in designed repeat proteins.Nucleic acids research · 2026Article
- Designing novel solenoid proteins with in silico evolution.Communications chemistry · 2025Article
- Reverse engineering of the pattern recognition receptor FLS2 reveals key design principles of broader recognition spectra against evading flg22 epitopes.Nature plants · 2025Article
- GeomeTRe: accurate calculation of geometrical descriptors of tandem repeat proteins.Bioinformatics (Oxford, England) · 2025Article
- Structure-aware annotation of leucine-rich repeat domains.PLoS computational biology · 2024Article
- De novo design of alpha-beta repeat proteins.bioRxiv : the preprint server for biology · 2024Article
- Targeting NLRP3 inflammasome for neurodegenerative disorders.Molecular psychiatry · 2023Review
- Hallucination of closed repeat proteins containing central pockets.Nature structural & molecular biology · 2023Article
- Structure-Aware Annotation of Leucine-rich Repeat Domains.bioRxiv : the preprint server for biology · 2023Article
- De novo design of knotted tandem repeat proteins.Nature communications · 2023Article
- Unusual structural and functional features of TpLRR/BspA-like LRR proteins.Journal of structural biology · 2023Review
- Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site.Journal of the American Chemical Society · 2023Article
- Protein design via deep learning.Briefings in bioinformatics · 2022Review
- Article
- Design of functionalised circular tandem repeat proteins with longer repeat topologies and enhanced subunit contact surfaces.Communications biology · 2021Article
- Synthesis and applications of anisotropic nanoparticles with precisely defined dimensions.Nature reviews. Chemistry · 2021Review
- Beyond natural: synthetic expansions of botanical form and function.The New phytologist · 2020Review
- Protein Engineering for Improving and Diversifying Natural Product Biosynthesis.Trends in biotechnology · 2020Review
- Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020Review
- Multi-input chemical control of protein dimerization for programming graded cellular responses.Nature biotechnology · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Shape complementarity is an important component of molecular recognition, and the ability to precisely adjust the shape of a binding scaffold to match a target of interest would greatly facilitate the creation of high-affinity protein reagents and therapeutics. Here we describe a general approach to control the shape of the binding surface on repeat-protein scaffolds and apply it to leucine-rich-repeat proteins. First, self-compatible building-block modules are designed that, when polymerized, generate surfaces with unique but constant curvatures. Second, a set of junction modules that connect the different building blocks are designed. Finally, new proteins with custom-designed shapes are generated by appropriately combining building-block and junction modules. Crystal structures of the designs illustrate the power of the approach in controlling repeat-protein curvature.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.