Leucine-rich repeat transmembrane

At least 12 ditferent TLRs have so far been identified in mammals (Uematsu and Akria 2007). TLRs are type I transmembrane PRRs that possess an extracellular domain contaiiung leucine-rich repeats (LRR), a transmembrane domain, and an... 

Figure 33.1 Toll-like receptor. Each receptor comprises a set of 18 or more leucine-rich repeat sequences, followed by a cysteine-rich domain, a single transmembrane helix, and a TIR (Toll-interleukin 1 receptor) domain that functions in signal transduction.

Membrane import machinery protein mas6 yeast was predicted with a maximum of only two short transmembrane helices 101-116 and 201-215, instead of four expected, but with many potential amphipathic P-strands. High peak in P-amphipathicity just next to the LDL or IDI motif is found at the mas6 yeast residue 69, mpcp rat (from mitochondrial carrier family) residue 83 and achl xenla residue 350. Observed amphipathic P-structure of a leucine rich repeat peptide LRP32 also contains LDL motif [99]. This motif may be important... 

TLRs are transmembrane receptors comprising an extracellular leucine-rich repeat and a cytoplasmic Toll/interleukin-1 receptor (TIR) domain, which are connected through a transmembrane domain [4]. The TIR domain is structurally homologous... 

TLRs are type I transmembrane proteins that consist of three major domains (1) a leucine-rich repeat (LRR) extracellular domain, (2) a transmembrane domain, and (3) a cytoplasmic TIR domain. There are 10 human TLRs (TLRl-10) and 13 murine TLRs (TLRl-13, although TLRIO is not functional in mice because of a retroviral insertion) that each have a different PAMP specificity. TLRl-10 are conserved between humans and mice, but TLRll-13 are not present in humans. Thus, despite some... 

The neurotrophins are unusual among polypeptide growth factors in that two different transmembrane proteins serve as receptors for each neurotrophin. The structural features of Trk tyrosine kinases and the p75 neurotrophin receptor are displayed in Fig. 1. The Trk subfamily of receptor tyrosine kinases is distinguished by immunoglobulin-C2 domains and repeats rich in leucine and cysteine residues in the extracellular domain and a tyrosine kinase domain with a small interruption and a short cytoplasmic tail. 

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