Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain
By J. Choe, M. Kelker, Ian A. Wilson. Science, 2005
618 citations recorded by the source corpus.
Subfields: Immunology, Microbiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/33fce8db0e89089abefd8e5aa4d58323904097db
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In Immunology
- Shizuo Akira
- O. Takeuchi
- Satoshi Uematsu
- Misako Matsumoto
- Tsukasa Seya
- Taro Kawai
- R. Medzhitov
- Jie-Oh Lee
In Microbiology
In Molecular Biology
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- O. Takeuchi
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- Misako Matsumoto
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- Taro Kawai
Citations in the corpus
- Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. (2007, neutral): “(Figure S7). As a control, TLR3 structures determined independently by two research groups were superimposed, and their average Ca rms difference was 1.1 A˚ (Bell et al., 2005; Choe et al., 2005 ).”
- Pathogen recognition and innate immunity. (2006, positive): “However, the threedimensional structure of the human TLR3 LRR motifs has recently been elucidated, and its structure suggests a somewhat different model in which negatively charged dsRNA is more likely to bind the outside convex surface of TLR3 (Choe et al., 2005).”
- TLR3: interferon induction by double-stranded RNA including poly(I:C). (2008, background): “TLR3 molecules are arranged as dimers in the crystals, and the C-terminal highly-conserved surface residues and a TLR3-specific LRR insertion at LRR20 forms a homodimer interface [21].”
- Pattern recognition receptors and inflammation. (2010, background): “The crystal structure of TLR3 bound to dsRNA revealed that dsRNA binds to the N-terminal and C-terminal portions of TLR3 LRRs, and this ligand binding dimerizes two TLR3 molecules (Choe et al., 2005; Liu et al., 2008).”
- Plant NBS-LRR proteins: adaptable guards (2006, background): “different types of dimers have been observed, involving interactions of either their concave surfaces [35] or their convex surfaces [36,37], or by concatenation involving an antiparallel -sheet at the interface [38].”