ArticleBMC microbiology2010
A nested leucine rich repeat (LRR) domain: the precursor of LRRs is a ten or eleven residue motif.
Article in BMC microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 59 citations in OpenAlex.
- NOD-like receptors in fish: evolution, structure, immune signaling, and targeting for aquaculture vaccine adjuvants.Frontiers in immunology · 2025Review
- Three-Dimensional Modeling of CpG DNA Binding with Matrix Lumican Shows Leucine-Rich Repeat Motif Involvement as in TLR9-CpG DNA Interactions.International journal of molecular sciences · 2023Article
- Intersections between innate immune response and gastric cancer development.World journal of gastroenterology · 2023Review
- Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.Scientific reports · 2022Article
- LRR-protein RNH1 dampens the inflammasome activation and is associated with COVID-19 severity.Life science alliance · 2022Article
- Structural and functional implications of leucine-rich repeats in toll-like receptor1 subfamily.Journal of biosciences · 2022Article
- Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans.Journal of cell communication and signaling · 2021Review
- Toll-Like Receptors: General Molecular and Structural Biology.Journal of immunology research · 2021Review
- Shrinking of repeating unit length in leucine-rich repeats from double-stranded DNA viruses.Archives of virology · 2021Article
- Structural and Evolutionary Adaptation of NOD-Like Receptors in Birds.BioMed research international · 2021Article
- Insights into the evolution of extracellular leucine-rich repeats in metazoans with special reference to Toll-like receptor 4.Journal of biosciences · 2019Article
- Identification and characterization of known and novel microRNAs in strawberry fruits induced by Botrytis cinerea.Scientific reports · 2018Article
- Enteric bacteria boost defences against oxidative stress in Entamoeba histolytica.Scientific reports · 2018Article
- Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity.Biomolecules · 2015Review
- On the origin and evolution of plant brassinosteroid receptor kinases.Journal of molecular evolution · 2014Article
- The past, present, and future of immune repertoire biology - the rise of next-generation repertoire analysis.Frontiers in immunology · 2013Review
- Comprehensive survey and genomic characterization of Toll-like receptors (TLRs) in channel catfish, Ictalurus punctatus: identification of novel fish TLRs.Immunogenetics · 2013Article
- Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants.Biomolecules · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLeucine rich repeats (LRRs) are present in over 60,000 proteins that have been identified in viruses, bacteria, archae, and eukaryotes. All known structures of repeated LRRs adopt an arc shape. Most LRRs are 20-30 residues long. All LRRs contain LxxLxLxxNxL, in which "L" is Leu, Ile, Val, or Phe and "N" is Asn, Thr, Ser, or Cys and "x" is any amino acid. Seven classes of LRRs have been identified. However, other LRR classes remains to be characterized. The evolution of LRRs is not well understood.
resultsHere we describe a novel LRR domain, or nested repeat observed in 134 proteins from 54 bacterial species. This novel LRR domain has 21 residues with the consensus sequence of LxxLxLxxNxLxxLDLxx(N/L/Q/x)xx or LxxLxCxxNxLxxLDLxx(N/L/x)xx. This LRR domain is characterized by a nested periodicity; it consists of alternating 10- and 11- residues units of LxxLxLxxNx(x/-). We call it "IRREKO" LRR, since the Japanese word for "nested" is "IRREKO". The first unit of the "IRREKO" LRR domain is frequently occupied by an "SDS22-like" LRR with the consensus of LxxLxLxxNxLxxLxxLxxLxx or a "Bacterial" LRR with the consensus of LxxLxLxxNxLxxLPxLPxx. In some proteins an "SDS22-like" LRR intervenes between "IRREKO" LRRs.
conclusionProteins having "IRREKO" LRR domain are almost exclusively found in bacteria. It is suggested that IRREKO@LRR evolved from a common ancestor with "SDS22-like" and "Bacterial" classes and that the ancestor of IRREKO@LRR is 10 or 11 residues of LxxLxLxxNx(x/-). The "IRREKO" LRR is predicted to adopt an arc shape with smaller curvature in which β-strands are formed on both concave and convex surfaces.
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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.