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Article

Reconstructing the TIR Side of the Myddosome: a Paradigm for TIR-TIR Interactions.

Structure (London, England : 1993) - 1 Mar 2016

Vyncke Laurens, Bovijn Celia, Pauwels Ewald, Van Acker Tim, Ruyssinck Elien, Burg Elianne, Tavernier Jan, Peelman Frank

Abstract excerpt

Members of the Toll-like receptor and interleukin-1 (IL-1) receptor families all signal via Toll/IL-1R (TIR) domain-driven assemblies with adaptors such as MyD88. We here combine the mammalian two-hybrid system MAPPIT and saturation mutagenesis to complement and extend crystallographic and nuclear magnetic resonance data, and reveal how TIR domains interact. We fully delineate the interaction sites on the MyD88...

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Source

Identifiers

PMID: 26876098
DOI: 10.1016/j.str.2015.12.018

Genes

TLR4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Reconstructing the TIR Side of the Myddosome: a Paradigm for TIR-TIR Interactions.PMID 26876098Read ↗

Identification of binding sites for myeloid differentiation primary response gene 88 (MyD88) and Toll-like receptor 4 in MyD88 adapter-like (Mal).Semantic proximity Read ↗

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Mal, more than a bridge to MyD88Semantic proximity Read ↗

Conformational dynamics of cancer-associated MyD88-TIR domain mutant L252P (L265P) allosterically tilts the landscape toward homo-dimerization.Semantic proximity Read ↗

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Structural Complementarity of Toll/Interleukin-1 Receptor Domains in Toll-like Receptors and the Adaptors Mal and MyD88Semantic proximity Read ↗

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Effects of Pathological Mutations on the Prion-Like Polymerisation of MyD88Semantic proximity Read ↗

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Interactive sites in the MyD88 Toll/interleukin (IL) 1 receptor domain responsible for coupling to the IL1beta signaling pathway.Semantic proximity Read ↗

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