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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5734
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pubmed:dateCreated |
2005-7-25
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pubmed:databankReference |
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pubmed:abstractText |
Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/TLR3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 3,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
22
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
581-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15961631-Amino Acid Motifs,
pubmed-meshheading:15961631-Amino Acid Sequence,
pubmed-meshheading:15961631-Binding Sites,
pubmed-meshheading:15961631-Crystallography, X-Ray,
pubmed-meshheading:15961631-Dimerization,
pubmed-meshheading:15961631-Glycosylation,
pubmed-meshheading:15961631-Humans,
pubmed-meshheading:15961631-Hydrogen Bonding,
pubmed-meshheading:15961631-Leucine,
pubmed-meshheading:15961631-Ligands,
pubmed-meshheading:15961631-Membrane Glycoproteins,
pubmed-meshheading:15961631-Models, Molecular,
pubmed-meshheading:15961631-Molecular Sequence Data,
pubmed-meshheading:15961631-Protein Conformation,
pubmed-meshheading:15961631-Protein Structure, Tertiary,
pubmed-meshheading:15961631-RNA, Double-Stranded,
pubmed-meshheading:15961631-Receptors, Cell Surface,
pubmed-meshheading:15961631-Repetitive Sequences, Amino Acid,
pubmed-meshheading:15961631-Signal Transduction,
pubmed-meshheading:15961631-Static Electricity,
pubmed-meshheading:15961631-Surface Properties,
pubmed-meshheading:15961631-Toll-Like Receptor 3,
pubmed-meshheading:15961631-Toll-Like Receptors
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pubmed:year |
2005
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pubmed:articleTitle |
Crystal structure of human toll-like receptor 3 (TLR3) ectodomain.
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pubmed:affiliation |
Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute (TSRI), 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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