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• W1964531685 endingPage "124" @default.
• W1964531685 startingPage "124" @default.
• W1964531685 abstract "Toll-like receptors (TLRs) play a central role in innate immunity. TLRs are membrane glycoproteins and contain leucine rich repeat (LRR) motif in the ectodomain. TLRs recognize and respond to molecules such as lipopolysaccharide, peptidoglycan, flagellin, and RNA from bacteria or viruses. The LRR domains in TLRs have been inferred to be responsible for molecular recognition. All LRRs include the highly conserved segment, LxxLxLxxNxL, in which L is Leu, Ile, Val, or Phe and N is Asn, Thr, Ser, or Cys and x is any amino acid. There are seven classes of LRRs including typical (T) and bacterial (S). All known domain structures adopt an arc or horseshoe shape. Vertebrate TLRs form six major families. The repeat numbers of LRRs and their phasing in TLRs differ with isoforms and species; they are aligned differently in various databases. We identified and aligned LRRs in TLRs by a new method described here. The new method utilizes known LRR structures to recognize and align new LRR motifs in TLRs and incorporates multiple sequence alignments and secondary structure predictions. TLRs from thirty-four vertebrate were analyzed. The repeat numbers of the LRRs ranges from 16 to 28. The LRRs found in TLRs frequently consists of LxxLxLxxNxLxxLxxxxF/LxxLxx (T) and sometimes short motifs including LxxLxLxxNxLxxLPx(x)LPxx (S). The TLR7 family (TLR7, TLR8, and TLR9) contain 27 LRRs. The LRRs at the N-terminal part have a super-motif of STT with about 80 residues. The super-repeat is represented by STTSTTSTT or _TTSTTSTT. The LRRs in TLRs form one or two horseshoe domains and are mostly flanked by two cysteine clusters including two or four cysteine residue. Each of the six major TLR families is characterized by their constituent LRR motifs, their repeat numbers, and their patterns of cysteine clusters. The central parts of the TLR1 and TLR7 families and of TLR4 have more irregular or longer LRR motifs. These central parts are inferred to play a key role in the structure and/or function of their TLRs. Furthermore, the super-repeat in the TLR7 family suggests strongly that bacterial and typical LRRs evolved from a common precursor." @default.
• W1964531685 created "2016-06-24" @default.
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• W1964531685 creator A5052453881 @default.
• W1964531685 creator A5055077720 @default.
• W1964531685 creator A5080063741 @default.
• W1964531685 date "2007-01-01" @default.
• W1964531685 modified "2023-10-10" @default.
• W1964531685 title "Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors" @default.
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• W1964531685 doi "https://doi.org/10.1186/1471-2164-8-124" @default.
• W1964531685 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1899181" @default.
• W1964531685 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17517123" @default.
• W1964531685 hasPublicationYear "2007" @default.
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