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• W2792521424 abstract "Toll-like receptors (TLRs) are a unique category of pattern recognition receptors that recognize distinct pathogenic components, often utilizing the same set of downstream adaptors. Specific molecular features of extracellular, transmembrane (TM), and cytoplasmic domains of TLRs are crucial for coordinating the complex, innate immune signaling pathway. Here, we constructed a full-length structural model of TLR4-a widely studied member of the interleukin-1 receptor/TLR superfamily-using homology modeling, protein-protein docking, and molecular dynamics simulations to understand the differential domain organization of TLR4 in a membrane-aqueous environment. Results showed that each functional domain of the membrane-bound TLR4 displayed several structural transitions that are biophysically essential for plasma membrane integration. Specifically, the extracellular and cytoplasmic domains were partially immersed in the upper and lower leaflets of the membrane bilayer. Meanwhile, TM domains tilted considerably to overcome the hydrophobic mismatch with the bilayer core. Our analysis indicates an alternate dimerization or a potential oligomerization interface of TLR4-TM. Moreover, the helical properties of an isolated TM dimer partly agree with that of the full-length receptor. Furthermore, membrane-absorbed or solvent-exposed surfaces of the toll/interleukin-1 receptor domain are consistent with previous X-ray crystallography and biochemical studies. Collectively, we provided a complete structural model of membrane-bound TLR4 that strengthens our current understanding of the complex mechanism of receptor activation and adaptor recruitment in the innate immune signaling pathway." @default.
• W2792521424 created "2018-03-29" @default.
• W2792521424 creator A5000545845 @default.
• W2792521424 creator A5020674417 @default.
• W2792521424 creator A5063370931 @default.
• W2792521424 creator A5070919578 @default.
• W2792521424 date "2018-03-12" @default.
• W2792521424 modified "2023-10-12" @default.
• W2792521424 title "Computational Insight Into the Structural Organization of Full-Length Toll-Like Receptor 4 Dimer in a Model Phospholipid Bilayer" @default.
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• W2792521424 doi "https://doi.org/10.3389/fimmu.2018.00489" @default.
• W2792521424 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5857566" @default.
• W2792521424 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29593733" @default.
• W2792521424 hasPublicationYear "2018" @default.
• W2792521424 type Work @default.
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• W2792521424 hasAuthorship W2792521424A5000545845 @default.
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• W2792521424 hasAuthorship W2792521424A5063370931 @default.
• W2792521424 hasAuthorship W2792521424A5070919578 @default.

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