TLR 1

TLR 1 is a member of the Toll-like receptor family (TLR) of pattern recognition receptors of the innate immune system.cite journal | author = Rock FL, Hardiman G, Timans JC, Kastelein RA, Bazan JF | title = A family of human receptors structurally related to Drosophila Toll | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 2 | pages = 588–93 | year = 1998 | month = January | pmid = 9435236 | pmc = 18464 | doi = 9435236 | url = | issn = ] cite journal | author = Lien E, Ingalls RR | title = Toll-like receptors | journal = Crit. Care Med. | volume = 30 | issue = 1 Suppl | pages = S1–11 | year = 2002 | month = January | pmid = 11782555 | doi = | url = http://www.ccmjournal.com/pt/re/ccm/abstract.00003246-200201001-00001.htm | issn = ] 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.cite web | url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7096 | title = SRF serum response factor | author = | authorlink = | coauthors = | date = | format = | work = Entrez Gene | publisher = National Center for Biotechnology Information, National Institutes of Health| pages = | language = | archiveurl = | archivedate = | quote = | accessdate = ]

TLR1 recognises peptidoglycan and (diacyl) lipoproteins in concert with TLR2 (as a heterodimer).cite journal | author = Farhat K, Riekenberg S, Heine H, Debarry J, Lang R, Mages J, Buwitt-Beckmann U, Röschmann K, Jung G, Wiesmüller KH, Ulmer AJ | title = Heterodimerization of TLR2 with TLR1 or TLR6 expands the ligand spectrum but does not lead to differential signaling | journal = J. Leukoc. Biol. | volume = 83 | issue = 3 | pages = 692–701 | year = 2008 | month = March | pmid = 18056480 | doi = 10.1189/jlb.0807586 | url = | issn = ] cite journal | author = Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO| title = Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide | journal = Cell | volume = 130 | issue = 6 | pages = 1071–82 | year = 2007 | month = September | pmid = 17889651 | doi = 10.1016/j.cell.2007.09.008 | url = | issn = ] It is found on the surface of macrophages and neutrophils.

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