Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-8-11
pubmed:abstractText
Toll-like receptors (TLRs) play central roles in the innate immune response by recognizing conserved structural patterns in diverse microbial molecules. The structures of the extracellular domains of four TLRs and their complexes with ligands have recently been determined by high-resolution X-ray crystallography. In this review, we describe these structures and discuss proposed activation mechanisms. TLRs deviate substantially from the canonical LRR structure and interact with a large variety of ligands in a highly divergent fashion. Agonistic ligands induce the formation of 'm' shaped TLR dimers in which the C-termini of the extracellular domains converge in the middle. This structural rearrangement of the extracellular domains suggests an activation mechanism that may be common to all TLR family proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0952-7915
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
414-9
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Structures of TLR-ligand complexes.
pubmed:affiliation
Department of Chemistry and Institute for the Bio-Century, KAIST, 373-1 Kusong-dong, Yusong-gu, Daejeon, Republic of Korea.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't