Leucine-rich repeats and pathogen recognition in Toll-like receptors

来自 dx.doi.org

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作者：

JK Bell，GED Mullen，CA Leifer，A Mazzoni，DR Davies，DM Segal

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摘要：

Toll-like receptors (TLRs) are the major cell-surface initiators of inflammatory responses to pathogens. They bind a wide variety of pathogenic substances through their ectodomains (ECDs). Here, we ask: what is the structural basis for this interaction? Toll-like receptor ECDs comprise 19–25 tandem copies of a motif known as the leucine-rich repeat (LRR). No X-ray structure of a TLR-ECD is currently available but there are several high-resolution LRR-containing proteins that can be used to model TLRs. We suggest that the basic framework of TLRs is a horseshoe-shaped solenoid that contains an extensive β-sheet on its concave surface, and numerous ligand-binding insertions. Together, these insertions and the β-sheet could provide a binding surface that is 10-fold greater in area than binding surfaces in antibodies and T-cell receptors.

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关键词：

Animals Humans Membrane Glycoproteins Receptors, Cell Surface Sequence Alignment Repetitive Sequences, Amino Acid Protein Structure, Tertiary Immunity, Cellular Amino Acid Sequence Molecular Sequence Data