ArticleBioMed research international2013
Elucidation of novel structural scaffold in rohu TLR2 and its binding site analysis with peptidoglycan, lipoteichoic acid and zymosan ligands, and downstream MyD88 adaptor protein.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Gastrointestinal Fate and Receptor-Mediated Mechanism of GPSGPQGSR, an Intestinal Barrier-Protective Collagen Peptide from ALASKA Pollock Skin.Marine drugs · 2026Article
- A novel alternative for pyrogen detection based on a transgenic cell line.Signal transduction and targeted therapy · 2024Article
- An Update on Toll-like Receptor 2, Its Function and Dimerization in Pro- and Anti-Inflammatory Processes.International journal of molecular sciences · 2023Review
- Molecular characterization of four innate immune genes inFish and shellfish immunology reports · 2022Article
- Novel Biomimetic Human TLR2-Derived Peptides for Potential Targeting of Lipoteichoic Acid: An In Silico Assessment.Biomedicines · 2021Article
- Structure of fish Toll-like receptors (TLR) and NOD-like receptors (NLR).International journal of biological macromolecules · 2020Review
- Article
- Directing the immune system with chemical compounds.ACS chemical biology · 2014Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toll-like receptors (TLRs) play key roles in sensing wide array of microbial signatures and induction of innate immunity. TLR2 in fish resembles higher eukaryotes by sensing peptidoglycan (PGN) and lipoteichoic acid (LTA) of bacterial cell wall and zymosan of yeasts. However, in fish TLR2, no study yet describes the ligand binding motifs in the leucine rich repeat regions (LRRs) of the extracellular domain (ECD) and important amino acids in TLR2-TIR (toll/interleukin-1 receptor) domain that could be engaged in transmitting downstream signaling. We predicted these in a commercially important freshwater fish species rohu (Labeo rohita) by constructing 3D models of TLR2-ECD, TLR2-TIR, and MyD88-TIR by comparative modeling followed by 40 ns (nanosecond) molecular dynamics simulation (MDS) for TLR2-ECD and 20 ns MDS for TLR2-TIR and MyD88-TIR. Protein (TLR2-ECD)-ligands (PGN, LTA, and zymosan) docking in rohu by AutoDock4.0, FlexX2.1, and GOLD4.1 anticipated LRR16-19, LRR12-14, and LRR20-CT as the most important ligand binding motifs. Protein (TLR2-TIR)-protein (MyD88-TIR) interaction by HADDOCK and ZDOCK predicted BB loop, α B-helix, α C-helix, and CD loop in TLR2-TIR and BB loop, α B-helix, and CD loop in MyD88-TIR as the critical binding domains. This study provides ligands recognition and downstream signaling.
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