| pubmed-article:15961631 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15961631 | lifeskim:mentions | umls-concept:C1313494 | lld:lifeskim |
| pubmed-article:15961631 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15961631 | lifeskim:mentions | umls-concept:C1336635 | lld:lifeskim |
| pubmed-article:15961631 | pubmed:issue | 5734 | lld:pubmed |
| pubmed-article:15961631 | pubmed:dateCreated | 2005-7-25 | lld:pubmed |
| pubmed-article:15961631 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15961631 | 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. | lld:pubmed |
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| pubmed-article:15961631 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15961631 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15961631 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15961631 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15961631 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:15961631 | pubmed:author | pubmed-author:WilsonIan AIA | lld:pubmed |
| pubmed-article:15961631 | pubmed:author | pubmed-author:ChoeJungwooJ | lld:pubmed |
| pubmed-article:15961631 | pubmed:author | pubmed-author:KelkerMatthew... | lld:pubmed |
| pubmed-article:15961631 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15961631 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:15961631 | pubmed:volume | 309 | lld:pubmed |
| pubmed-article:15961631 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15961631 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15961631 | pubmed:pagination | 581-5 | lld:pubmed |
| pubmed-article:15961631 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:15961631 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15961631 | pubmed:articleTitle | Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. | lld:pubmed |
| pubmed-article:15961631 | 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. | lld:pubmed |
| pubmed-article:15961631 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15961631 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15961631 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15961631 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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