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Article

Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.

Cell - 7 Sept 2007

Kim Ho Min, Park Beom Seok, Kim Jung-In, Kim Sung Eun, Lee Judong, Oh Se Cheol, Enkhbayar Purevjav, Matsushima Norio, Lee Hayyoung, Yoo Ook Joon, Lee Jie-Oh

Abstract excerpt

TLR4 and MD-2 form a heterodimer that recognizes LPS (lipopolysaccharide) from Gram-negative bacteria. Eritoran is an analog of LPS that antagonizes its activity by binding to the TLR4-MD-2 complex. We determined the structure of the full-length ectodomain of the mouse TLR4 and MD-2 complex. We also produced a series of hybrids of human TLR4 and hagfish VLR and determined their structures with and without bound...

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Source

Identifiers

PMID: 17803912
DOI: 10.1016/j.cell.2007.08.002

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.

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