Six human homologs of the Drosophila Toll receptor were initially identified based on their sequence similarities ａnd designated toll-like receptors (TLR). Toll receptors are involved in mediating dorsoventral polarization in the developing Drosophila embryo ａnd participate in the host immunity. The TLR family of proteins are characterized by a highly conserved Toll homology (TH) domain, which is essential for Toll-induced signal transduction. TLR1, as well as the other TLR family members, are type I transmembrane receptors that characteristically contain an extracellular domain consisting of several leucine-rich regions along with a single cylasmic Toll / IL-1R-like domain. TLR2 ａnd TLR4 are activated in response to lipopolysacchride (LPS) stimulation, which results in the activation ａnd translocation of NFkB ａnd suggests that these receptors are involved in mediating inflammatory responses. Expression of TLR receptors is highest in peripheral blood leukocytes, macro-phages, ａnd TLR6 is highly homologous to TLR1, sharing greater than 65% sequence identity, and, like other members of TLR family, it induces NFkB signaling upon activation.
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Peptide

ICCIHCFCWB

HumanMouseRat