ArticleProtein science : a publication of the Protein Society2014
Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment.
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 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- De novo design of alpha-beta repeat proteins.bioRxiv : the preprint server for biology · 2024Article
- Designed leucine-rich repeat proteins bind two muramyl dipeptide ligands.Protein science : a publication of the Protein Society · 2021Article
- The use of consensus sequence information to engineer stability and activity in proteins.Methods in enzymology · 2020Article
- Exome sequencing in multiple sclerosis families identifies 12 candidate genes and nominates biological pathways for the genesis of disease.PLoS genetics · 2019Article
- COPs and POPs Patrol Inflammasome Activation.Journal of molecular biology · 2018Review
- Structural Insights into VLR Fine Specificity for Blood Group Carbohydrates.Structure (London, England : 1993) · 2017Article
- Consensus protein design.Protein engineering, design & selection : PEDS · 2016Review
- A designed repeat protein as an affinity capture reagent.Biochemical Society transactions · 2015Review
- Control of repeat-protein curvature by computational protein design.Nature structural & molecular biology · 2015Article
- A general computational approach for repeat protein design.Journal of molecular biology · 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 at 1 institution in 1 country.
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Abstract
Repeat proteins have recently emerged as especially well-suited alternative binding scaffolds due to their modular architecture and biophysical properties. Here we present the design of a scaffold based on the consensus sequence of the leucine rich repeat (LRR) domain of the NOD family of cytoplasmic innate immune system receptors. Consensus sequence design has emerged as a protein design tool to create de novo proteins that capture sequence-structure relationships and interactions present in nature. The multiple sequence alignment of 311 individual LRRs, which are the putative ligand-recognition domain in NOD proteins, resulted in a consensus sequence protein containing two internal and N- and C-capping repeats named CLRR2. CLRR2 protein is a stable, monomeric, and cysteine free scaffold that without any affinity maturation displays micromolar binding to muramyl dipeptide, a bacterial cell wall fragment. To our knowledge, this is the first report of direct interaction of a NOD LRR with a physiologically relevant ligand.
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