Toll-like receptor 2

UniProt data

UniProt name: TLR2_HUMAN (O60603)

Gene name: TLR2; Synonyms=TIL4

Organism: Homo sapiens (Human).

Function: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins (PubMed:10426996). Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6 (PubMed:11441107). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36). The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). {ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:10426996, ECO:0000269|PubMed:11441107, ECO:0000269|PubMed:15809303, ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:19362712}.

Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:16880211}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. Triacylated lipoproteins induce the same mechanism for TLR2:TLR1 heterodimers. {ECO:0000269|PubMed:16880211}.

Transmembrane domains:

  1. 589-609, 21 AA, Helical. {ECO:0000255}.

Sequence: 784 AA

10 20 30 40 50 60 MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL TEAVKSLDLS 70 80 90 100 110 120 NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG SLEHLDLSYN YLSNLSSSWF 130 140 150 160 170 180 KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK LQILRVGNMD TFTKIQRKDF AGLTFLEELE 190 200 210 220 230 240 IDASDLQSYE PKSLKSIQNV SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS 250 260 270 280 290 300 ELSTGETNSL IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN 310 320 330 340 350 360 DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL VPCLLSQHLK 370 380 390 400 410 420 SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA SLEKTGETLL TLKNLTNIDI 430 440 450 460 470 480 SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK 490 500 510 520 530 540 ELYISRNKLM TLPDASLLPM LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE 550 560 570 580 590 600 FLSFTQEQQA LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL 610 620 630 640 650 660 LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER DAYWVENLMV 670 680 690 700 710 720 QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV FVLSENFVKS EWCKYELDFS 730 740 750 760 770 780 HFRLFDENND AAILILLEPI EKKAIPQRFC KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA AIKS

CATM prediction

The sequence of TLR2_HUMAN returned 2 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
      590       600       610
    |    +    |    +    |  		 (Å) (°) (Å) (°)  
Model 1 HRTALVSGMCCALFLLILLTGVLCHRF 7.1 -40.0° 4.5 43.9 -23.3
Model 2 HRTALVSGMCCALFLLILLTGVLCHRF 7.4 -49.9° 2.8 47.1 -12.1

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 590, LEU, HA A, 589, ALA, O 2.92Å
B, 593, GLY, HA1 A, 590, LEU, O 3.28Å
A, 590, LEU, HA B, 589, ALA, O 2.92Å
A, 593, GLY, HA1 B, 590, LEU, O 3.28Å