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Toll-like receptor 1

PDB rendering based on 1fyv.
Available structures
1fyv, 2z7x
Symbols TLR1; CD281; DKFZp547I0610; DKFZp564I0682; KIAA0012; MGC104956; MGC126311; MGC126312; TIL; rsc786
External IDs OMIM601194 MGI1341295 HomoloGene20694 GeneCards: TLR1 Gene
RNA expression pattern
PBB GE TLR1 210176 at tn.png
More reference expression data
Species Human Mouse
Entrez 7096 21897
Ensembl ENSG00000174125 ENSMUSG00000044827
UniProt Q15399 Q6A0E8
RefSeq (mRNA) XM_001129777 NM_030682
RefSeq (protein) XP_001129777 NP_109607
Location (UCSC) Chr 4:
38.47 - 38.48 Mb
Chr 5:
65.2 - 65.21 Mb
PubMed search [1] [2]

TLR 1 is a member of the Toll-like receptor family (TLR) of pattern recognition receptors of the innate immune system.[1][2] TLR1 recognizes pathogen-associated molecular pattern with a specificity for gram-positive bacteria. TLR1 has also been designated as CD281 (cluster of differentiation 281).

TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This gene is ubiquitously expressed, and at higher levels than other TLR genes. Different length transcripts presumably resulting from use of alternative polyadenylation site, and/or from alternative splicing, have been noted for this gene.[3]

TLR1 recognises peptidoglycan and (triacyl) lipoproteins in concert with TLR2 (as a heterodimer).[4][5] It is found on the surface of macrophages and neutrophils.


TLR 1 has been shown to interact with TLR 2.[6]


  1. ^ Rock FL, Hardiman G, Timans JC, Kastelein RA, Bazan JF (January 1998). "A family of human receptors structurally related to Drosophila Toll". Proc. Natl. Acad. Sci. U.S.A. 95 (2): 588–93. doi:9435236. PMID 9435236.  
  2. ^ Lien E, Ingalls RR (January 2002). "Toll-like receptors". Crit. Care Med. 30 (1 Suppl): S1–11. doi:10.1097/00003246-200201001-00001. PMID 11782555.  
  3. ^ "SRF serum response factor". Entrez Gene. National Center for Biotechnology Information, National Institutes of Health.  
  4. ^ Farhat K, Riekenberg S, Heine H, Debarry J, Lang R, Mages J, Buwitt-Beckmann U, Röschmann K, Jung G, Wiesmüller KH, Ulmer AJ (March 2008). "Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling". J. Leukoc. Biol. 83 (3): 692–701. doi:10.1189/jlb.0807586. PMID 18056480.  
  5. ^ Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO (September 2007). "Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide". Cell 130 (6): 1071–82. doi:10.1016/j.cell.2007.09.008. PMID 17889651.  
  6. ^ Takeuchi, Osamu; Sato Shintaro, Horiuchi Takao, Hoshino Katsuaki, Takeda Kiyoshi, Dong Zhongyun, Modlin Robert L, Akira Shizuo (Jul. 2002). "Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins". J. Immunol. (United States) 169 (1): 10–4. ISSN 0022-1767. PMID 12077222.  

External links

This article incorporates text from the United States National Library of Medicine ([3]), which is in the public domain.



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