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Titel:

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.

Dokumenttyp:
Journal Article
Autor(en):
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...     »
Zeitschriftentitel:
J Biol Chem
Jahr:
2003
Band / Volume:
278
Heft / Issue:
41
Seitenangaben Beitrag:
39822-9
Sprache:
eng
Volltext / DOI:
doi:10.1074/jbc.M304766200
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/12860988
Print-ISSN:
0021-9258
TUM Einrichtung:
Institut für Medizinische Mikrobiologie, Immunologie und Hygiene
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