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Title:

Cellular recognition of tri-/di-palmitoylated peptides is independent from a domain encompassing the N-terminal seven leucine-rich repeat (LRR)/LRR-like motifs of TLR2.

Document type:
Journal Article
Author(s):
Meng, G; Grabiec, A; Vallon, M; Ebe, B; Hampel, S; Bessler, W; Wagner, H; Kirschning, CJ
Abstract:
Toll-like receptors (TLRs) mediate microbial pattern recognition in vertebrates. A broad variety of agonists has been attributed to TLR2 and three TLRs, TLR4, TLR2, and TLR5, have been demonstrated to bind microbial products. Distinct agonists might interact with different subdomains of the TLR2 extracellular domain. The TLR2 extracellular domain sequence includes 10 canonical leucine-rich repeat (LRR) motifs and 8-10 additional and potentially functionally relevant LRR-like motifs. Thus, the tr...     »
Journal title abbreviation:
J Biol Chem
Year:
2003
Journal volume:
278
Journal issue:
41
Pages contribution:
39822-9
Language:
eng
Fulltext / DOI:
doi:10.1074/jbc.M304766200
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/12860988
Print-ISSN:
0021-9258
TUM Institution:
Institut für Medizinische Mikrobiologie, Immunologie und Hygiene
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