|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
2007-9-6
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
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 MD-2 and Eritoran. TLR4 is an atypical member of the LRR family and is composed of N-terminal, central, and C-terminal domains. The beta sheet of the central domain shows unusually small radii and large twist angles. MD-2 binds to the concave surface of the N-terminal and central domains. The interaction with Eritoran is mediated by a hydrophobic internal pocket in MD-2. Based on structural analysis and mutagenesis experiments on MD-2 and TLR4, we propose a model of TLR4-MD-2 dimerization induced by LPS.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-O-decyl-2-deoxy-6-O-(2-deoxy-3-O-(...,
http://linkedlifedata.com/resource/pubmed/chemical/Disaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Fish Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/LY96 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Ly96 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Antigen 96,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sugar Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/TLR4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tlr4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 4
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0092-8674
|
|
pubmed:author |
pubmed-author:EnkhbayarPurevjavP,
pubmed-author:KimHo MinHM,
pubmed-author:KimJung-InJI,
pubmed-author:KimSung EunSE,
pubmed-author:LeeHayyoungH,
pubmed-author:LeeJie-OhJO,
pubmed-author:LeeJudongJ,
pubmed-author:MatsushimaNorioN,
pubmed-author:OhSe CheolSC,
pubmed-author:ParkBeom SeokBS,
pubmed-author:YooOok JoonOJ
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
7
|
|
pubmed:volume |
130
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
906-17
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:17803912-Amino Acid Sequence,
pubmed-meshheading:17803912-Animals,
pubmed-meshheading:17803912-Binding Sites,
pubmed-meshheading:17803912-Cloning, Molecular,
pubmed-meshheading:17803912-Crystallography, X-Ray,
pubmed-meshheading:17803912-Dimerization,
pubmed-meshheading:17803912-Disaccharides,
pubmed-meshheading:17803912-Fish Proteins,
pubmed-meshheading:17803912-Hagfishes,
pubmed-meshheading:17803912-Humans,
pubmed-meshheading:17803912-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:17803912-Immunoglobulin Variable Region,
pubmed-meshheading:17803912-Lipopolysaccharides,
pubmed-meshheading:17803912-Lymphocyte Antigen 96,
pubmed-meshheading:17803912-Mice,
pubmed-meshheading:17803912-Models, Molecular,
pubmed-meshheading:17803912-Molecular Sequence Data,
pubmed-meshheading:17803912-Molecular Structure,
pubmed-meshheading:17803912-Mutation,
pubmed-meshheading:17803912-Protein Binding,
pubmed-meshheading:17803912-Protein Conformation,
pubmed-meshheading:17803912-Protein Engineering,
pubmed-meshheading:17803912-Protein Structure, Tertiary,
pubmed-meshheading:17803912-Recombinant Fusion Proteins,
pubmed-meshheading:17803912-Structural Homology, Protein,
pubmed-meshheading:17803912-Sugar Phosphates,
pubmed-meshheading:17803912-Toll-Like Receptor 4
|
|
pubmed:year |
2007
|
|
pubmed:articleTitle |
Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.
|
|
pubmed:affiliation |
Department of Chemistry, Korea Advanced Institute of Science and Technology, Daejon, Korea 305-701.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
